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The Protein Folding Problem
Open accessAbstract
The "protein folding problem" consists of three closely related puzzles: (a) What is the folding code? (b) What is the folding mechanism? (c) Can we predict the native structure of a protein from its amino acid sequence? Once regarded as a grand challenge, protein folding has seen great progress in recent years. Now, foldable proteins and nonbiological polymers are being designed routinely and moving toward successful applications. The structures of small proteins are now often well predicted by computer methods. And, there is now a testable explanation for how a protein can fold so quickly: A protein solves its large global optimization problem as a series of smaller local optimization problems, growing and assembling the native structure from peptide fragments, local structures first.
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“The statistical energy landscape theory was developed to study protein folding.1,128–131”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [130]
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“AlphaFold does not resolve the decades-long protein folding challenge, nor does it identify the folding pathways.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [51]
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“Levinthal argued that there is no need to search this vast space since the energy landscape is funnel-like, rather than flat, and thus can guide sampling toward the biological conformational basin.”
From AlphaFold, Artificial Intelligence (AI), and Allostery (2022) · cites this paper as [51]
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Cites
A Second Generation Force Field for the Simulation of Proteins, Nucleic Acids, and Organic Molecules
Cornell, W. D., Cieplak, P., Bayly, C. I., Gould, I. R., Merz, K. M., Ferguson, D. M., Spellmeyer, D. C., Fox, T., Caldwell, J. W., & Kollman, P. A. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00124a002 · Cited by 13,111
Comparative Protein Modelling by Satisfaction of Spatial Restraints
Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
THE weighted histogram analysis method for free‐energy calculations on biomolecules. I. The method
Kumar, S., Rosenberg, J. M., Bouzida, D., Swendsen, R. H., & Kollman, P. A. (1992) · Journal of Computational Chemistry · doi:10.1002/jcc.540130812 · Cited by 6,808
Replica-exchange molecular dynamics method for protein folding
Sugita, Y., & Okamoto, Y. (1999) · Chemical Physics Letters · doi:10.1016/s0009-2614(99)01123-9 · Cited by 4,499
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,829
Self-citationPrediction of protein conformation
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a002 · Cited by 3,309
Empirical Predictions of Protein Conformation
Chou, P. Y., & Fasman, G. D. (1978) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.47.070178.001343 · Cited by 3,137
The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
Pauling, L. C., Corey, R. B., & Branson, H. R. (1951) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.37.4.205 · Cited by 3,007
Gellman, S. H. (1998) · Accounts of Chemical Research · doi:10.1021/ar960298r · Cited by 2,550
The relation between the divergence of sequence and structure in proteins.
Chothia, C., & Lesk, A. M. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04288.x · Cited by 2,458
From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
Self-citationMcCammon, J., Gelin, B., & Karplus, M. (1977) · Nature · doi:10.1038/267585a0 · Cited by 1,972
Progressive sequence alignment as a prerequisitetto correct phylogenetic trees
Feng, D.-F., & Doolittle, R. F. (1987) · Journal of Molecular Evolution · doi:10.1007/bf02603120 · Cited by 1,883
Design of a Novel Globular Protein Fold with Atomic-Level Accuracy
Kuhlman, B. A., Dantas, G. A., Ireton, G. C., Varani, G., Stoddard, B. L., & Baker, D. A. (2003) · Science · doi:10.1126/science.1089427 · Cited by 1,666
Spin glasses and the statistical mechanics of protein folding.
Bryngelson, J. D., & Wolynes, P. G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.21.7524 · Cited by 1,647
Protein Structure Prediction and Structural Genomics
Baker, D., & Sali, A. (2001) · Science · doi:10.1126/science.1065659 · Cited by 1,587
Principles of protein folding — A perspective from simple exact models
Dill, K. A., Bromberg, S., Yue, K., Chan, H. S., Fiebig, K. M., Yee, D. P., & Thomas, P. D. (1995) · Protein Science · doi:10.1002/pro.5560040401 · Cited by 1,529
Self-citationPlaxco, K. W., Simons, K. T., & Baker, D. A. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1645 · Cited by 1,515
Monte Carlo-minimization approach to the multiple-minima problem in protein folding.
Li, Z., & Scheraga, H. A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6611 · Cited by 1,475
Duan, Y., & Kollman, P. A. (1998) · Science · doi:10.1126/science.282.5389.740 · Cited by 1,337
Theory for the folding and stability of globular proteins
Dill, K. A. (1985) · Biochemistry · doi:10.1021/bi00327a032 · Cited by 1,256
Self-citationClementi, C., Nymeyer, H., & Onuchic, J. N. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3693 · Cited by 1,228
A new approach to protein fold recognition
Jones, D. T., Taylort, W. R., & Thornton, J. M. (1992) · Nature · doi:10.1038/358086a0 · Cited by 1,221
Molecular dynamics and protein function
Karplus, M., & Kuriyan, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408930102 · Cited by 1,159
De Novo Protein Design: Fully Automated Sequence Selection
Dahiyat, B. I., & Mayo, S. L. (1997) · Science · doi:10.1126/science.278.5335.82 · Cited by 1,156
ModBase, a database of annotated comparative protein structure models, and associated resources
Pieper, U., Webb, B., Barkan, D. T., Schneidman‐Duhovny, D., Schlessinger, A., Braberg, H., Yang, Z., Meng, E., Pettersen, E. F., Huang, C. C., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1091 · Cited by 1,073
Hydrogen bonding and biological specificity analysed by protein engineering
Fersht, A. R., Shi, J., Knill-Jones, J. W., Lowe, D. M., Wilkinson, A. J., Blow, D. M., Brick, P., Carter, P. M., Waye, M. M. Y., & Winter, G. P. (1985) · Nature · doi:10.1038/314235a0 · Cited by 1,056
Kim, P. S., & Baldwin, R. L. (1982) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.51.070182.002331 · Cited by 1,036
Experimental and Theoretical Aspects of Protein Folding
Anfinsen, C. B., & Scheraga, H. A. (1975) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60413-1 · Cited by 973
A lattice statistical mechanics model of the conformational and sequence spaces of proteins
Lau, K. F., & Dill, K. A. (1989) · Macromolecules · doi:10.1021/ma00200a030 · Cited by 954
Self-citationProtein folding funnels: a kinetic approach to the sequence-structure relationship.
Leopold, P., Montal, M., & Onuchic, J. N. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.18.8721 · Cited by 929
Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
Schuler, B., Lipman, E. A., & Eaton, W. A. (2002) · Nature · doi:10.1038/nature01060 · Cited by 921
Foldamers as versatile frameworks for the design and evolution of function
Goodman, C. M., Choi, S., Shandler, S. J., & DeGrado, W. F. (2007) · Nature Chemical Biology · doi:10.1038/nchembio876 · Cited by 899
Toward High-Resolution de Novo Structure Prediction for Small Proteins
Bradley, P. H., Misura, K. M. S., & Baker, D. A. (2005) · Science · doi:10.1126/science.1113801 · Cited by 865
The protein folding ‘speed limit’
Kubelka, J., Hofrichter, J., & Eaton, W. A. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.01.013 · Cited by 832
Molecular evolution by staggered extension process (StEP) in vitro recombination
Zhao, H., Giver, L., Shao, Z., Affholter, J. A., & Arnold, F. H. (1998) · Nature Biotechnology · doi:10.1038/nbt0398-258 · Cited by 757
Itzhaki, L. S., Otzen, D. E., & Fersht, A. R. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0616 · Cited by 750
Protein Design by Binary Patterning of Polar and Nonpolar Amino Acids
Kamtekar, S., Schiffer, J. M., Xiong, H., Babik, J. M., & Hecht, M. H. (1993) · Science · doi:10.1126/science.8259512 · Cited by 731
Mapping the transition state and pathway of protein folding by protein engineering
Matouschek, A. T., Kellis, J. T., Serrano, L., & Fersht, A. R. (1989) · Nature · doi:10.1038/340122a0 · Cited by 703
Non-haemolytic β-amino-acid oligomers
Porter, E. A., Wang, X., Lee, H., Weisblum, B., & Gellman, S. H. (2000) · Nature · doi:10.1038/35007145 · Cited by 671
Computational design of receptor and sensor proteins with novel functions
Looger, L. L., Dwyer, M. A., Smith, J. J., & Hellinga, H. W. (2003) · Nature · doi:10.1038/nature01556 · Cited by 668
Direct Observation of the Three-State Folding of a Single Protein Molecule
Cecconi, C., Shank, E. A., Bustamante, C., & Marqusee, S. (2005) · Science · doi:10.1126/science.1116702 · Cited by 635
Chodera, J. D., Singhal, N., Pande, V. S., Dill, K. A., & Swope, W. C. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2714538 · Cited by 633
Self-citationAll-Atom Structure Prediction and Folding Simulations of a Stable Protein
Simmerling, C. L., Strockbine, B., & Roitberg, A. E. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0273851 · Cited by 593
Wang, L., Xie, J., & Schultz, P. G. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.101105.121507 · Cited by 584
A large‐scale experiment to assess protein structure prediction methods
Moult, J., Pedersen, J. T., Judson, R., & Fidelis, K. (1995) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340230303 · Cited by 555
Screen Savers of the World Unite!
Shirts, M., & Pande, V. (2000) · Science · doi:10.1126/science.290.5498.1903 · Cited by 550
Nucleation mechanisms in protein folding
Fersht, A. R. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80002-4 · Cited by 545
Reaction coordinates and rates from transition paths
Best, R. B., & Hummer, G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408098102 · Cited by 514
Is protein folding hierarchic? I. Local structure and peptide folding
Baldwin, R. L., & Rose, G. D. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01346-2 · Cited by 492
A decade of CASP: progress, bottlenecks and prognosis in protein structure prediction
Moult, J. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.05.011 · Cited by 485
Shea, J.-E., & Brooks III, C. L. (2001) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.52.1.499 · Cited by 481
On the transition coordinate for protein folding
Du, R., Pande, V., Grosberg, A., Tanaka, T., & Shakhnovich, E. (1998) · The Journal of Chemical Physics · doi:10.1063/1.475393 · Cited by 479
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR
Korzhnev, D. M., Salvatella, X., Vendruscolo, M., Nardo, A. A. D., Davidson, A. R., Dobson, C. M., & Kay, L. E. (2004) · Nature · doi:10.1038/nature02655 · Cited by 478
Cooperativity in protein-folding kinetics.
Dill, K. A., Fiebig, K. M., & Chan, H. S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1942 · Cited by 477
Self-citationGrantcharova, V., Alm, E. J., Baker, D. A., & Horwich, A. L. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00176-7 · Cited by 474
Describing Protein Folding Kinetics by Molecular Dynamics Simulations. 1. Theory
Swope, W., Pitera, J., & Suits, F. (2004) · The Journal of Physical Chemistry B · doi:10.1021/jp037421y · Cited by 451
Protein folding dynamics: The diffusion‐collision model and experimental data
Karplus, M., & Weaver, D. L. (1994) · Protein Science · doi:10.1002/pro.5560030413 · Cited by 447
Atomic Coordinates and Structure Factors for Two Helical Configurations of Polypeptide Chains
Pauling, L. C., & Corey, R. B. (1951) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.37.5.235 · Cited by 422
Polymer principles and protein folding
Dill, K. A. (1999) · Protein Science · doi:10.1110/ps.8.6.1166 · Cited by 422
Self-citationContext-dependent secondary structure formation of a designed protein sequence
Minor, D. L., & Kim, P. S. (1996) · Nature · doi:10.1038/380730a0 · Cited by 393
Hecht, M. H., Richardson, J. S., Richardson, D. C., & Ogden, R. C. (1990) · Science · doi:10.1126/science.2392678 · Cited by 391
Hansmann, U. H. E., & Okamoto, Y. (1993) · Journal of Computational Chemistry · doi:10.1002/jcc.540141110 · Cited by 387
The origins of asymmetry in the folding transition states of protein L and protein G
Karanicolas, J., & Brooks, C. L. (2002) · Protein Science · doi:10.1110/ps.0205402 · Cited by 379
Noé, F., Horenko, I., Schütte, C., & Smith, J. (2007) · Journal of Chemical Physics · doi:10.1063/1.2714539 · Cited by 377
Helical Peptoid Mimics of Magainin-2 Amide
Patch, J. A., & Barron, A. E. (2003) · Journal of the American Chemical Society · doi:10.1021/ja037320d · Cited by 375
Molecular dynamics of native protein
Levitt, M. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80304-0 · Cited by 361
The speed limit for protein folding measured by triplet–triplet energy transfer
Bieri, O., Wirz, J., Hellrung, B., Schutkowski, M., Drewello, M., & Kiefhaber, T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9597 · Cited by 358
Φ-Value analysis and the nature of protein-folding transition states
Fersht, A. R., & Sato, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402684101 · Cited by 351
Hydrogen exchange methods to study protein folding
Krishna, M. C. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.005 · Cited by 350
Completeness in structural genomics.
Vitkup, D., Melamud, E., Moult, J., & Sander, C. (2001) · Nature Structural Biology · doi:10.1038/88640 · Cited by 349
Origins of structure in globular proteins.
Chan, H. S., & Dill, K. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.16.6388 · Cited by 345
Self-citationUnderstanding folding and design: Replica-exchange simulations of ``Trp-cage'' miniproteins
Pitera, J. W., & Swope, W. C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1330954100 · Cited by 344
Protein Folding Theory: From Lattice to All-Atom Models
Mirny, L., & Shakhnovich, E. (2001) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.30.1.361 · Cited by 341
The role of hydrophobic interactions in initiation and propagation of protein folding
Dyson, H. J., Wright, P. E., & Scheraga, H. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605504103 · Cited by 330
Mukhopadhyay, S., Krishnan, R., Lemke, E. A., Lindquist, S. L., & Deniz, A. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611503104 · Cited by 316
Experimental Identification of Downhill Protein Folding
García‐Mira, M. M., Sadqi, M., Fischer, N., Sánchez‐Ruiz, J. M., & Muñoz, V. (2002) · Science · doi:10.1126/science.1077809 · Cited by 307
Free energy landscape of protein folding in water: Explicit vs. implicit solvent
Zhou, R. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10483 · Cited by 301
Gromiha, M. M., & Selvaraj, S. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4775 · Cited by 297
Design of DNA-Binding Peptides Based on the Leucine Zipper Motif
O’Neil, K. T., Hoess, R. H., & DeGrado, W. F. (1990) · Science · doi:10.1126/science.2389143 · Cited by 296
Protein folding: The stepwise assembly of foldon units
Maity, H., Maity, M., Mallela, K. M. G., Mayne, L. C., & Englander, S. W. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501043102 · Cited by 295
Žagrović, B., Snow, C. D., Shirts, M. R., & Pande, V. S. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00997-x · Cited by 288
Transition states and folding dynamics of proteins and heteropolymers
Chan, H. S., & Dill, K. A. (1994) · The Journal of Chemical Physics · doi:10.1063/1.466677 · Cited by 282
Self-citationAnatomy of energetic changes accompanying urea-induced protein denaturation
Auton, M. T., Holthauzen, L. M. F., & Bolen, D. W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706251104 · Cited by 277
Singhal, N., Snow, C. D., & Pande, V. S. (2004) · The Journal of Chemical Physics · doi:10.1063/1.1738647 · Cited by 271
De novo proteins from designed combinatorial libraries
Hecht, M. H., Das, A., Go, A., Bradley, L. H., & Wei, Y. (2004) · Protein Science · doi:10.1110/ps.04690804 · Cited by 268
Sub-microsecond Protein Folding
Kubelka, J., Chiu, T. K., Davies, D. R., Eaton, W. A., & Hofrichter, J. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.03.034 · Cited by 255
Blue Gene: A vision for protein science using a petaflop supercomputer
Allen, F. E., Almasi, G. S., Andreoni, W., Beece, D. K., Berne, B. J., Bright, A. A., Brunheroto, J. R., Caşcaval, C., Castaños, J. G., Coteus, P., et al. (2001) · IBM Systems Journal · doi:10.1147/sj.402.0310 · Cited by 254
Dynamics of Unfolded Polypeptide Chains as Model for the Earliest Steps in Protein Folding
Krieger, F., Fierz, B., Bieri, O., Drewello, M., & Kiefhaber, T. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00892-1 · Cited by 251
Folding free-energy landscape of villin headpiece subdomain from molecular dynamics simulations
Lei, H., Wu, C. F., Liu, H., & Duan, Y. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608432104 · Cited by 248
Atom-by-atom analysis of global downhill protein folding
Sadqi, M., Fushman, D., & Muñoz, V. (2006) · Nature · doi:10.1038/nature04859 · Cited by 247
Unifying features in protein-folding mechanisms
Gianni, S., Guydosh, N. R., Khan, F., Caldas, T. D., Mayor, U., White, G. W. N., DeMarco, M. L., Daggett, V., & Fersht, A. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1835776100 · Cited by 241
Respective roles of short- and long-range interactions in protein folding.
Gō, N., & Taketomi, H. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.2.559 · Cited by 235
Shea, J., Onuchic, J. N., & Brooks, C. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12512 · Cited by 231
Maxwell, K. L., Wildes, D. P., Zarrine‐Afsar, A., Rios, M. A. D. L., Brown, A. G., Friel, C. T., Hedberg, L., Horng, J., Bona, D., Miller, E. J., et al. (2005) · Protein Science · doi:10.1110/ps.041205405 · Cited by 229
Side-chain Interactions Governing the Pairing of Half-cystine Residues in Ribonuclease
Haber, E., & Anfinsen, C. B. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)73945-3 · Cited by 223
Probing structural heterogeneities and fluctuations of nucleic acids and denatured proteins
Laurence, T. A., Kong, X., Jäger, M., & Weiss, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508584102 · Cited by 222
Preorganized secondary structure as an important determinant of fast protein folding.
Myers, J. K., & Oas, T. G. (2001) · Nature Structural Biology · doi:10.1038/88626 · Cited by 221
P versus Q : Structural reaction coordinates capture protein folding on smooth landscapes
Cho, S. S., Levy, Y., & Wolynes, P. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509768103 · Cited by 220
Different folding transition states may result in the same native structure
Viguera, A. R., Serrano, L. G., & Wilmanns, M. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb1096-874 · Cited by 219
Gilmanshin, R., Williams, S., Callender, R. H., Woodruff, W. H., & Dyer, R. B. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3709 · Cited by 213
MODBASE, a database of annotated comparative protein structure models, and associated resources
Pieper, U. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkh095 · Cited by 213
Designing polymers that mimic biomolecules
Kirshenbaum, K., Zuckermann, R. N., & DILL, K. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80075-x · Cited by 209
Self-citationThermal stabilities of globular proteins
Dill, K. A., Alonso, D. O. V., & Hutchinson, K. (1989) · Biochemistry · doi:10.1021/bi00439a019 · Cited by 208
Self-citationFAST EVENTS IN PROTEIN FOLDING: The Time Evolution of Primary Processes
Callender, R. H., Dyer, R. B., Gilmanshin, R., & Woodruff, W. H. (1998) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.49.1.173 · Cited by 203
Gibson, K. D., & Scheraga, H. A. (1967) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.58.2.420 · Cited by 198
Unfolded conformations of α-lytic protease are more stable than its native state
Sohl, J. L., Jaswal, S. S., & Agard, D. A. (1998) · Nature · doi:10.1038/27470 · Cited by 197
Prediction of protein folding rates from the amino acid sequence-predicted secondary structure
Ivankov, D. N., & Finkelstein, A. V. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402659101 · Cited by 189
A Method for Predicting Nucleation Sites for Protein Folding Based on Hydrophobic Contacts
Matheson, R. R., & Scheraga, H. A. (1978) · Macromolecules · doi:10.1021/ma60064a038 · Cited by 187
TASSER: An automated method for the prediction of protein tertiary structures in CASP6
Zhang, Y., Arakaki, A. K., & Skolnick, J. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20724 · Cited by 185
Diffusion–collision model for protein folding
Karplus, M., & Weaver, D. L. (1979) · Biopolymers · doi:10.1002/bip.1979.360180608 · Cited by 183
Folding Rate Prediction Using Total Contact Distance
Zhou, H., & Zhou, Y. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75410-6 · Cited by 181
Protein folding under confinement: A role for solvent
Lucent, D., Vishal, V., & Pande, V. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608256104 · Cited by 171
Unger, R., & Moult, J. (1993) · Bulletin of Mathematical Biology · doi:10.1016/s0092-8240(05)80169-7 · Cited by 169
Swope, W. C., Pitera, J. W., Suits, F., Pitman, M. C., Eleftheriou, M., Fitch, B. G., Germain, R. S., Rayshubskiy, A., Ward, T. J. C., Zhestkov, Y., et al. (2004) · The Journal of Physical Chemistry B · doi:10.1021/jp037422q · Cited by 169
Ab initio Folding Simulation of the Trp-cage Mini-protein Approaches NMR Resolution
Chowdhury, S., Lee, M. C., Xiong, G., & Duan, Y. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00177-3 · Cited by 169
α‐Helix‐forming propensities in peptides and proteins
Creamer, T. P., & Rose, G. D. (1994) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340190202 · Cited by 167
The Three-Dimensional Structure of a Protein Molecule
Kendrew, J. C. (1961) · Scientific American · doi:10.1038/scientificamerican1261-96 · Cited by 166
Role of Solvent in Determining Conformational Preferences of Alanine Dipeptide in Water
Drozdov, A. N., Grossfield, A. M., & Pappu, R. V. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039051x · Cited by 166
Effect of Viscosity on the Kinetics of α-Helix and β-Hairpin Formation
Jas, G. S., Eaton, W. A., & Hofrichter, J. (2000) · The Journal of Physical Chemistry B · doi:10.1021/jp0022048 · Cited by 166
Jayachandran, G., Vishal, V., & Pande, V. S. (2006) · The Journal of Chemical Physics · doi:10.1063/1.2186317 · Cited by 165
Némethy, G., & Scheraga, H. A. (1965) · Biopolymers · doi:10.1002/bip.360030205 · Cited by 161
An experimentally determined protein folding energy landscape
Mello, C. C., & Barrick, D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403386101 · Cited by 159
Segel, D. J., Bachmann, A., Hofrichter, J., Hodgson, K. O., Doniach, S., & Kiefhaber, T. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2703 · Cited by 157
Folding a Nonbiological Polymer into a Compact Multihelical Structure
Lee, B.-C., Zuckermann, R. N., & Dill, K. A. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0514904 · Cited by 156
Self-citationSequence space, folding and protein design
Cordes, M. H. J., Davidson, A. R., & Sauer, R. T. (1996) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(96)80088-1 · Cited by 154
De novo design of a Zn2+-binding protein
Handel, T. M., & DeGrado, W. F. (1990) · Journal of the American Chemical Society · doi:10.1021/ja00174a039 · Cited by 154
Makarov, D. E., Keller, C. A., Plaxco, K. W., & Metiu, H. I. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052713599 · Cited by 150
Ołdziej, S., Czaplewski, C. R., Liwo, A., Chinchio, M., Nanias, M., Vila, J. A., Khalili, M., Arnautova, Y. A., Jagielska, A., Makowski, M., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502655102 · Cited by 149
Origin of Unusual φ-values in Protein Folding: Evidence Against Specific Nucleation Sites
Sanchez, I. E., & Kiefhaber, T. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.10.016 · Cited by 148
FOLD-RATE: prediction of protein folding rates from amino acid sequence
Gromiha, M. M., Thangakani, A. M., & Selvaraj, S. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl043 · Cited by 147
Protein folding by zipping and assembly
Ozkan, S. B., Wu, G. A., Chodera, J. D., & Dill, K. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703700104 · Cited by 147
Self-citationKlepeis, J. L., & Floudas, C. A. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74640-2 · Cited by 146
Transition states and the meaning of Phi-values in protein folding kinetics.
Ozkan, S. B., Bahar, İ., & Dill, K. A. (2001) · Nature Structural Biology · doi:10.1038/nsb0901-765 · Cited by 143
Self-citationFolding units in globular proteins.
Lesk, A. M., & Rose, G. D. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.7.4304 · Cited by 141
Robust Proofs of NP-Hardness for Protein Folding: General Lattices and Energy Potentials
Hart, W. E., & Istrail, S. (1997) · Journal of Computational Biology · doi:10.1089/cmb.1997.4.1 · Cited by 139
Felts, A. K., Harano, Y., Gallicchio, E., & Levy, R. M. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20104 · Cited by 136
EVA: Large-scale analysis of secondary structure prediction
Rost, B., & Eyrich, V. A. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10051 · Cited by 134
Protein Structures and Optimal Folding from a Geometrical Variational Principle
Micheletti, C., Banavar, J. R., Maritan, A., & Seno, F. (1999) · Physical Review Letters · doi:10.1103/physrevlett.82.3372 · Cited by 127
Coarse Master Equation from Bayesian Analysis of Replica Molecular Dynamics Simulations
Sriraman, S., Kevrekidis, I. G., & Hummer, G. (2005) · The Journal of Physical Chemistry B · doi:10.1021/jp046448u · Cited by 127
Wallace, I. M., Blackshields, G., & Higgins, D. G. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.04.002 · Cited by 126
Malleability of protein folding pathways: a simple reason for complex behaviour
Lindberg, M. O., & Oliveberg, M. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.01.008 · Cited by 126
The sequences of small proteins are not extensively optimized for rapid folding by natural selection
Kim, D. E., Gu, H., & Baker, D. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.4982 · Cited by 123
(2005) · Science · doi:10.1126/science.309.5731.78b · Cited by 122
Bachmann, A., & Kiefhaber, T. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4399 · Cited by 120
Assessment of predictions submitted for the CASP6 comparative modeling category
Tress, M. L., Ezkurdia, I., Graña‐Castro, O., López, G., & Valencia, A. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20720 · Cited by 119
Deechongkit, S., Dawson, P. E., & Kelly, J. W. (2004) · Journal of the American Chemical Society · doi:10.1021/ja045934s · Cited by 118
Wolfenden, R. V. (2007) · The Journal of General Physiology · doi:10.1085/jgp.200709743 · Cited by 118
Assessment of progress over the CASP experiments
Venclovas, ?., Zemla, A. T., Fidelis, K. A., & Moult, J. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10530 · Cited by 116
Validation of an All-Atom Protein Force Field: From Dipeptides to Larger Peptides
Gnanakaran, S., & Garcı́a, A. E. (2003) · The Journal of Physical Chemistry B · doi:10.1021/jp0359079 · Cited by 115
Cytochrome c folding pathway: Kinetic native-state hydrogen exchange
Hoang, L., Bédard, S., Mallela, K. M. G., Lin, Y., & Englander, S. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152439199 · Cited by 115
Determination of a Transition State at Atomic Resolution from Protein Engineering Data
Paci, E., Vendruscolo, M., Dobson, C. M., & Karplus, M. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00944-0 · Cited by 114
Unger, R., & Moult, J. (1993) · Bulletin of Mathematical Biology · doi:10.1007/bf02460703 · Cited by 114
Folding kinetics of proteins and copolymers
Miller, R. M., Danko, C. A., Fasolka, M. J., Balazs, A. C., Chan, H. S., & Dill, K. A. (1992) · The Journal of Chemical Physics · doi:10.1063/1.462462 · Cited by 113
Self-citationMallela, K. M. G., Maity, H., Rumbley, J. N., Lin, Y., & Englander, S. W. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.04.035 · Cited by 113
Muñoz, V., & Sánchez‐Ruiz, J. M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405829101 · Cited by 113
Differences in the folding transition state of ubiquitin indicated by φ and ψ analyses
Sosnick, T. R., Dothager, R. S., & Krantz, B. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407683101 · Cited by 112
A protein folding pathway with multiple folding intermediates at atomic resolution
Feng, H., Zhou, Z., & Bai, Y. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501372102 · Cited by 112
Banavar, J. R., & Maritan, A. (2007) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.36.040306.132808 · Cited by 112
Protein core assembly processes
Fiebig, K. M., & Dill, K. A. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464068 · Cited by 111
Self-citationUltra-fast Barrier-limited Folding in the Peripheral Subunit-binding Domain Family
Ferguson, N. S., Sharpe, T., Schartau, P. J., Sato, S., Allen, M. D., Johnson, C. M., Rutherford, T. J., & Fersht, A. R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.031 · Cited by 106
Seife, C. (2005) · Science · doi:10.1126/science.309.5731.78a · Cited by 104
Rational Development of β-Peptide Inhibitors of Human Cytomegalovirus Entry
English, E. P., Chumanov, R. S., Gellman, S. H., & Compton, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508485200 · Cited by 101
Folding Rates and Low-entropy-loss Routes of Two-state Proteins
Weikl, T. R., & Dill, K. A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00436-4 · Cited by 101
Self-citationGenetic Studies Of Protein Stability And Mechanisms Of Folding
Goldenberg, D. P. (1988) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.17.060188.002405 · Cited by 99
Distinguishing between cooperative and unimodal downhill protein folding
Huang, F. L., Sato, S., Sharpe, T., Ying, L., & Fersht, A. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609717104 · Cited by 99
Folding Very Short Peptides Using Molecular Dynamics
Ho, B. K., & Dill, K. A. (2006) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0020027 · Cited by 97
Self-citationChameleon sequences in the PDB
Mezei, M. (1998) · Protein Engineering Design and Selection · doi:10.1093/protein/11.6.411 · Cited by 95
Kinetic Pathways of β-Hairpin (Un)folding in Explicit Solvent
Bolhuis, P. G. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.048744 · Cited by 94
Multiple pathways on a protein-folding energy landscape: Kinetic evidence
Goldbeck, R. A., Thomas, Y. G., Chen, E., Esquerra, R. M., & Kliger, D. S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2782 · Cited by 90
Yoda, T., Sugita, Y., & Okamoto, Y. (2004) · Chemical Physics · doi:10.1016/j.chemphys.2004.08.002 · Cited by 89
Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding process
Matagne, A., Radford, S. E., & Dobson, C. M. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0963 · Cited by 88
Two-stage Folding of HP-35 from Ab Initio Simulations
Lei, H., & Duan, Y. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.040 · Cited by 87
Master Equation Approach to Protein Folding and Kinetic Traps
Cieplak, M., Henkel, M., Karbowski, J., & Banavar, J. R. (1998) · Physical Review Letters · doi:10.1103/physrevlett.80.3654 · Cited by 87
All-Atom Ab Initio Folding of a Diverse Set of Proteins
Yang, J. S., Chen, W. W., Skolnick, J., & Shakhnovich, E. I. (2007) · Structure · doi:10.1016/j.str.2006.11.010 · Cited by 86
Cymes, G. D., Grosman, C. F., & Auerbach, A. L. (2002) · Biochemistry · doi:10.1021/bi011864f · Cited by 86
The Role of Dipole Interactions in Determining Polypeptide Configurations
Brant, D. A., & Flory, P. J. (1965) · Journal of the American Chemical Society · doi:10.1021/ja01081a054 · Cited by 86
Packing Is a Key Selection Factor in the Evolution of Protein Hydrophobic Cores
Chen, J., & Stites, W. E. (2001) · Biochemistry · doi:10.1021/bi011776v · Cited by 84
Helical Peptoid Mimics of Lung Surfactant Protein C
Wu, C. W., Seurynck‐Servoss, S. L., Lee, K. Y. C., & Barron, A. E. (2003) · Chemistry & Biology · doi:10.1016/j.chembiol.2003.10.008 · Cited by 84
Naganathan, A. N., Pérez‐Jiménez, R., Sánchez‐Ruiz, J. M., & Muñoz, V. (2005) · Biochemistry · doi:10.1021/bi050118y · Cited by 84
Muñoz, V. (2002) · International Journal of Quantum Chemistry · doi:10.1002/qua.10384 · Cited by 81
Protein Folding Rates Estimated from Contact Predictions
Punta, M., & Rost, B. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.068 · Cited by 81
A Limiting Speed for Protein Folding at Low Solvent Viscosity
Qiu, L., & Hagen, S. J. (2004) · Journal of the American Chemical Society · doi:10.1021/ja049966r · Cited by 79
Energetic contribution of side chain hydrogen bonding to the stability of staphylococcal nuclease
Byrne, M. P., Manuel, R., Lowe, L. G., & Stites, W. E. (1995) · Biochemistry · doi:10.1021/bi00042a029 · Cited by 78
Tsai, C., Maizel, J. V., & Nussinov, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.22.12038 · Cited by 77
Experimental evaluation of topological parameters determining protein-folding rates
Miller, E. J., Fischer, K. F., & Marqusee, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162219099 · Cited by 77
Geometry and physics of proteins
Banavar, J. R., Maritan, A., Micheletti, C., & Trovato, A. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10091 · Cited by 75
The Ultimate Speed Limit to Protein Folding Is Conformational Searching
Ghosh, K., Ozkan, S. B., & Dill, K. A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja066785b · Cited by 74
Self-citationGoldenberg, D. P. (1999) · Nature Structural Biology · doi:10.1038/14866 · Cited by 72
Basin hopping simulations for all-atom protein folding
Verma, A., Schug, A. H., Lee, K. H., & Wenzel, W. (2006) · The Journal of Chemical Physics · doi:10.1063/1.2138030 · Cited by 71
Cooperativity in two‐state protein folding kinetics
Weikl, T. R., Palassini, M., & Dill, K. A. (2004) · Protein Science · doi:10.1110/ps.03403604 · Cited by 71
Self-citationPrediction and design of macromolecular structures and interactions
Baker, D. A. (2006) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2005.1803 · Cited by 71
Ab initio prediction of protein structure using LINUS
Srinivasan, R., & Rose, G. D. (2002) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10103 · Cited by 70
Shaping up the protein folding funnel by local interaction: Lesson from a structure prediction study
Chikenji, G., Fujitsuka, Y., & Takada, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508195103 · Cited by 69
Identification of the minimal protein-folding nucleus through loop-entropy perturbations
Lindberg, M. O., Haglund, E., Hubner, I. A., Shakhnovich, E. I., & Oliveberg, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508863103 · Cited by 68
The chicken–egg scenario of protein folding revisited
Uversky, V. N., & Fink, A. L. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02441-9 · Cited by 68
Knott, M., & Chan, H. S. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21066 · Cited by 67
Onuchic, J. N., & Wolynes, P. G. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464201 · Cited by 64
Friel, C. T., Beddard, G. S., & Radford, S. E. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.06.076 · Cited by 63
Research works printed but not linked: 2
- Grabowski M, 2007, Nucleic Acids Seq. Topol., 17, 347
- Hubner IA, 2003, Abstr. Pap. Am. Chem. Soc., 226, U450
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Metadata
- Authors
- Dill, K. A., Ozkan, S. B., Shell, M. S., & Weikl, T. R.
- Affiliations
- University of California, San Francisco (US)
- Arizona State University (US)
- University of California, Santa Barbara (US)
- Max Planck Institute of Colloids and Interfaces (DE)
- Venue
- Annual Review of Biophysics
- Publisher
- Annual Reviews
- Published
- 2008-06-01
- Volume
- 37
- Issue
- 1
- Pages
- 289-316
- ISSN
- 1936-122X (ISSN-L)
- 1936-1238
- PMC
- PMC2443096
- OpenAlex
- W2129020329
- Cited by
- 1,163
- References
- 248
- Citations by year
- 2026: 51 · 2025: 61 · 2024: 60 · 2023: 70 · 2022: 73 · 2021: 73 · 2020: 59 · 2019: 53 · 2018: 52 · 2017: 47 · 2016: 48 · 2015: 43 · 2014: 70 · 2013: 82 · 2012: 78
- FWCI
- 6.04
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Biophysics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Max Planck Digital Library (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (GM34993, R01GM034993)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- protein folding, folding mechanism, protein structure prediction, de novo protein design, peptide fragments, local optimization, global optimization, folding rate
- MeSH terms
- Computer Simulation, Models, Chemical, Models, Molecular, Protein Conformation, Proteins, Protein Folding
About these checks
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