Cited by 725Protein Structure and DynamicsChemical Synthesis and AnalysisRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.

Elucidating the folding problem of helical peptides using empirical parameters

Muñoz, Victor, Serrano, Luis·1994·Nature Structural & Molecular Biology

Open this paper in CoChat — free account

Abstract

Using an empirical analysis of experimental data we have estimated a set of energy contributions which accounts for the stability of isolated alpha-helices. With this database and an algorithm based on statistical mechanics, we describe the average helical behaviour in solution of 323 peptides and the helicity per residue of those peptides analyzed by nuclear magnetic resonance. Moreover the algorithm successfully detects the alpha-helical tendency, in solution, of a peptide corresponding to a beta-strand of ubiquitin.

Integrity signals

Registry

Crossref · 10.1038/nsb0694-399

Cites

94 of 94 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

NMR with Proteins and Nucleic Acids
Wüthrich, K. (1986) · Europhysics news · doi:10.1051/epn/19861701011 · Cited by 8,028
Statistical mechanics of chain molecules
Flory, P. J., & Volkenstein, M. V. (1969) · Biopolymers · doi:10.1002/bip.1969.360080514 · Cited by 6,449
NMR of Proteins and Nucleic Acids
(2006) · Royal Society of Chemistry eBooks · doi:10.1039/9781847555236-00336 · Cited by 5,874
Determination of the helix and β form of proteins in aqueous solution by circular dichroism
Chen, Y.-H., Yang, J. T., & Chau, K. H. (1974) · Biochemistry · doi:10.1021/bi00713a027 · Cited by 2,070
Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains
Zimm, B., & Bragg, J. K. (1959) · The Journal of Chemical Physics · doi:10.1063/1.1730390 · Cited by 1,801
Structure of ubiquitin refined at 1.8 A resolution.
Vijay-Kumar, S., Bugg, C., & Cook, W. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90679-6 · Cited by 1,636
Amino Acid Preferences for Specific Locations at the Ends of α Helices
Richardson, J. S., & Richardson, D. C. (1988) · Science · doi:10.1126/science.3381086 · Cited by 1,364
A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids
O’Neil, K. T., & DeGrado, W. F. (1990) · Science · doi:10.1126/science.2237415 · Cited by 1,186
Calculation of conformational ensembles from potentials of mena force
Sippl, M. J. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80269-4 · Cited by 1,068
A Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein G
Gronenborn, A. M., Filpula, D. R., Essig, N. Z., Achari, A., Whitlow, M. D., Wingfield, P. T., & Clore, G. M. (1991) · Science · doi:10.1126/science.1871600 · Cited by 816
Unusually stable helix formation in short alanine-based peptides.
Marqusee, S., Robbins, V. H., & Baldwin, R. L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5286 · Cited by 777
Signal transduction in bacteria
Stock, J. B., Stock, A., & Mottonen, J. M. (1990) · Nature · doi:10.1038/344395a0 · Cited by 676
Tests of the helix dipole model for stabilization of α-helices
Shoemaker, K. R., Kim, P. S., York, E. J., Stewart, J. M., & Baldwin, R. L. (1987) · Nature · doi:10.1038/326563a0 · Cited by 598
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide
Sönnichsen, F. D., Eyk, J. E. V., Hodges, R. S., & Sykes, B. D. (1992) · Biochemistry · doi:10.1021/bi00152a015 · Cited by 583
The ras protein family: evolutionary tree and role of conserved amino acids
Valencia, A., Chardin, P., Wittinghofer, A., & Sander, C. (1991) · Biochemistry · doi:10.1021/bi00233a001 · Cited by 569
Parameters of helix–coil transition theory for alanine‐based peptides of varying chain lengths in water
Scholtz, J. M., Qian, H., York, E. J., Stewart, J. M., & Baldwin, R. L. (1991) · Biopolymers · doi:10.1002/bip.360311304 · Cited by 502
Structural Basis of Amino Acid α Helix Propensity
Blaber, M., Zhang, X., & Matthews, B. W. (1993) · Science · doi:10.1126/science.8503008 · Cited by 475
Side Chain Contributions to the Stability of Alpha-Helical Structure in Peptides
Lyu, P. C., Liff, M. I., Marky, L. A., & Kallenbach, N. R. (1990) · Science · doi:10.1126/science.2237416 · Cited by 463
Relative helix-forming tendencies of nonpolar amino acids
Padmanabhan, S., Marqusee, S., Ridgeway, T. M., Laue, T. M., & Baldwin, R. L. (1990) · Nature · doi:10.1038/344268a0 · Cited by 462
PATHWAYS OF PROTEIN FOLDING
Matthews, C. R. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.003253 · Cited by 437
Folding of peptide fragments comprising the complete sequence of proteins
Dyson, H. J., Merutka, G., Waltho, J. P., Lerner, R. A., & Wright, P. E. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90633-u · Cited by 388
α-Helix stability in proteins
Serrano, L. G., Sancho, J., Hirshberg, M., & Fersht, A. R. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90906-z · Cited by 369
Self-citation
Capping and α-helix stability
Serrano, L., & Fersht, A. R. (1989) · Nature · doi:10.1038/342296a0 · Cited by 364
Self-citation
Structure of bacteriophage T4 lysozyme refined at 1.7 Å resolution
Weaver, L. H., & Matthews, B. W. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90636-x · Cited by 353
Large differences in the helix propensities of alanine and glycine
Chakrabartty, A., Schellman, J. A., & Baldwin, R. L. (1991) · Nature · doi:10.1038/351586a0 · Cited by 313
Helix-coil transition of the isolated amino terminus of ribonuclease
Brown, J. E., & Klee, W. A. (1971) · Biochemistry · doi:10.1021/bi00779a019 · Cited by 310
Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities
Chakrabartty, A., Kortemme, T., Padmanabhan, S., & Baldwin, R. L. (1993) · Biochemistry · doi:10.1021/bi00072a010 · Cited by 306
Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water.
Scholtz, J. M., Marqusee, S., Baldwin, R. L., York, E. J., Stewart, J. M., Santoro, M. M., & Bolen, D. W. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.7.2854 · Cited by 301
Helix stop signals in proteins and peptides: The capping box
Harper, E. T., & Rose, G. D. (1993) · Biochemistry · doi:10.1021/bi00081a001 · Cited by 298
Stabilization of alpha-helical structures in short peptides via end capping
Forood, B., Feliciano, E. J., & Nambiar, K. P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.3.838 · Cited by 235
Peptide conformation and protein folding
Dyson, H. J., & Wright, P. E. (1993) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(93)90203-w · Cited by 235
α-Helix stability in proteins
Horovitz, A., Matthews, J. M., & Fersht, A. R. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90907-2 · Cited by 216
The helix–coil transition in heterogeneous peptides with specific side‐chain interactions: Theory and comparison with CD spectral data
Gans, P. J., Lyu, P. C., Manning, M. C., Woody, R. W., & Kallenbach, N. R. (1991) · Biopolymers · doi:10.1002/bip.360311315 · Cited by 201
Analysis of the interaction between charged side chains and the .alpha.-helix dipole using designed thermostable mutants of phage T4 lysozyme
Nicholson, H., Anderson, D. E., Daopin, S., & Matthews, B. W. (1991) · Biochemistry · doi:10.1021/bi00105a002 · Cited by 177
Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helixes of myoglobin
Waltho, J. P., Feher, V. A., Merutka, G., Dyson, H. J., & Wright, P. E. (1993) · Biochemistry · doi:10.1021/bi00076a006 · Cited by 175
The folding of an enzyme
Serrano, L., Matouschek, A. T., & Fersht, A. R. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90566-3 · Cited by 168
Self-citation
A neutral, water-soluble, .alpha.-helical peptide: the effect of ionic strength on the helix-coil equilibrium
Scholtz, J. M., York, E. J., Stewart, J. M., & Baldwin, R. L. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00013a079 · Cited by 150
Further studies of the helix dipole model: Effects of a free α‐NH3+ or α‐COO− group on helix stability
Fairman, R., Shoemaker, K. R., York, E. J., Stewart, J. M., & Baldwin, R. L. (1989) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340050102 · Cited by 144
Effect of central-residue replacements on the helical stability of a monomeric peptide
Merutka, G., Lipton, W., Shalongo, W., Park, S. H., & Stellwagen, E. (1990) · Biochemistry · doi:10.1021/bi00484a021 · Cited by 124
Helical peptides with three pairs of Asp‐Arg and Glu‐Arg residues in different orientations and spacings
Huyghues‐Despointes, B. M. P., Scholtz, J. M., & Baldwin, R. L. (1993) · Protein Science · doi:10.1002/pro.5560020108 · Cited by 124
Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions.
Dasgupta, S., & Bell, J. A. (1993) · PubMed · Cited by 123
Histidine residues at the N- and C-termini of .alpha.-helixes: perturbed pKas and protein stability
Sancho, J., Serrano, L. G., & Fersht, A. R. (1992) · Biochemistry · doi:10.1021/bi00123a006 · Cited by 123
Self-citation
Effect of a single aspartate on helix stability at different positions in a neutral alanine‐based peptide
Huyghues‐Despointes, B. M. P., Scholtz, J. M., & Baldwin, R. L. (1993) · Protein Science · doi:10.1002/pro.5560021006 · Cited by 122
Design of helix ends
Dasgupta, S., & BELL, J. A. (1993) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1993.tb00470.x · Cited by 120
Capping interactions in isolated .alpha. helixes: position-dependent substitution effects and structure of a serine-capped peptide helix
Lyu, P. C., Wemmer, D. E., Zhou, H. X., Pinker, R. J., & Kallenbach, N. R. (1993) · Biochemistry · doi:10.1021/bi00053a006 · Cited by 119
Effect of end group blockage on the properties of a class A amphipathic helical peptide
Venkatachalapathi, Y. V., Phillips, M. C., Epand, R. M., Epand, R. F., Tytler, E. M., Segrest, J. P., & Anantharamaiah, G. M. (1993) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340150403 · Cited by 114
Kinetics of amide proton exchange in helical peptides of varying chain lengths. Interpretation by the Lifson-Roig equation
Rohl, C. A., Scholtz, J. M., York, E. J., Stewart, J. M., & Baldwin, R. L. (1992) · Biochemistry · doi:10.1021/bi00120a001 · Cited by 113
Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59
Bell, J. A., Becktel, W. J., Sauer, U. H., Baase, W. A., & Matthews, B. W. (1992) · Biochemistry · doi:10.1021/bi00129a006 · Cited by 108
Side‐chain interactions in the C‐peptide helix: Phe 8 His 12+
Shoemaker, K. R., Fairman, R., Schultz, D., Robertson, A. D., York, E. J., Stewart, J. M., & Baldwin, R. L. (1990) · Biopolymers · doi:10.1002/bip.360290104 · Cited by 107
Extracting information on folding from the amino acid sequence: Accurate predictions for protein regions with preferred conformation in the absence of tertiary interactions
Rooman, M. J., Kocher, J.-P. A., & Wodak, S. J. (1992) · Biochemistry · doi:10.1021/bi00157a009 · Cited by 106
Helix propagation in trifluoroethanol solutions
Storrs, R. W., Truckses, D. M., & Wemmer, D. E. (1992) · Biopolymers · doi:10.1002/bip.360321211 · Cited by 103
The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S‐peptide analogues with enhanced helical stability
Mitchinson, C., & Baldwin, R. L. (1986) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340010106 · Cited by 99
Residue helix parameters obtained from dichroic analysis of peptides of defined sequence
Park, S. H., Shalongo, W., & Stellwagen, E. (1993) · Biochemistry · doi:10.1021/bi00078a033 · Cited by 96
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate
Sancho, J., Neira, J. L., & Fersht, A. R. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90559-3 · Cited by 90
Effect of amino acid ion pairs on peptide helicity
Merutka, G., & Stellwagen, E. (1991) · Biochemistry · doi:10.1021/bi00220a021 · Cited by 89
Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin
Shin, H. C., Merutka, G., Waltho, J. P., Tennant, L. L., Dyson, H. J., & Wright, P. E. (1993) · Biochemistry · doi:10.1021/bi00076a008 · Cited by 85
Physical reasons for secondary structure stability: α‐Helices in short peptides
Finkelstein, A. V., Badretdinov, A. Y., & Ptitsyn, O. B. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340100403 · Cited by 85
Straight-chain non-polar amino acids are good helix-formers in water
Padmanabhan, S., & Baldwin, R. L. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90553-i · Cited by 82
1 H NMR and CD evidence of the folding of the isolated ribonuclease 50–61 fragment
Jiménez, M. A., Nieto, J. L., Herranz, J., Rico, M., & Santoro, J. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80948-1 · Cited by 78
Helix-Coil Stability Constants for the Naturally Occurring Amino Acids in Water. II. Characterization of the Host Polymers and Application of the Host-Guest Technique to Random Poly(hydroxypropylglutamine-co-hydroxybutylglutamine)
Dreele, P. H. V., Lotan, N., Ananthanarayanan, V. S., Andreatta, R. H., Poland, D. C., & Scheraga, H. A. (1971) · Macromolecules · doi:10.1021/ma60022a008 · Cited by 75
A theory of protein molecule self-organization
Finkelstein, A. V., & Ptitsyn, O. B. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90049-8 · Cited by 74
Residual helical structure in the C-terminal fragment of cytochrome c
Kuroda, Y. (1993) · Biochemistry · doi:10.1021/bi00056a004 · Cited by 73
Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal
Shin, H. C., Merutka, G., Waltho, J. P., Wright, P. E., & Dyson, H. J. (1993) · Biochemistry · doi:10.1021/bi00076a007 · Cited by 73
Prediction of the thermodynamics of protein unfolding: the helix-coil transition of poly(L-alanine).
Ooi, T., & Oobatake, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.7.2859 · Cited by 72
Position-dependent stabilizing effects in .alpha.-helices: N-terminal capping in synthetic model peptides
Lyu, P. C., Zhou, H. X., Jelveh, N., Wemmer, D. E., & Kellenbach, N. R. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00042a047 · Cited by 69
CD and 1H‐NMR studies on the conformational properties of peptide fragments from the C‐terminal domain of thermolysin
Jiménez, M. A., Bruix, M., González, C., Blanco, F. J., NIETO, J. L., Herranz, J. F., & Rico, M. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17584.x · Cited by 68
A single-stranded amphipathic .alpha.-helix in aqueous solution: Design, structural characterization, and its application for determining .alpha.-helical propensities of amino acids
Zhou, N., Kay, C. M., Sykes, B. D., & Hodges, R. S. (1993) · Biochemistry · doi:10.1021/bi00075a011 · Cited by 68
Positional independence and additivity of amino acid replacements on helix stability in monomeric peptides
Merutka, G., & Stellwagen, E. (1990) · Biochemistry · doi:10.1021/bi00456a007 · Cited by 60
The contribution of residue ion pairs to the helical stability of a model peptide
Stellwagen, E., Park, S.-H., Shalongo, W., & Jain, A. (1992) · Biopolymers · doi:10.1002/bip.360320909 · Cited by 59
Effect of the substitution Ala .fwdarw. Gly at each of five residue positions in the C-peptide helix
Strehlow, K. G., & Baldwin, R. L. (1989) · Biochemistry · doi:10.1021/bi00431a025 · Cited by 55
The role of ion pairs in .alpha. helix stability: two new designed helical peptides
Lyu, P., Marky, L. A., & Kallenbach, N. R. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00189a067 · Cited by 54
Folding of a peptide corresponding to the .alpha.-helix in bovine pancreatic trypsin inhibitor
Goodman, E. M., & Kim, P. S. (1989) · Biochemistry · doi:10.1021/bi00436a033 · Cited by 52
X-Ray Analysis of Ferredoxin from Spirulina platensis
Tomitake Tsukihara, A., Fukuyama, K., TAHARA, H., Katsube, Y., Matsuura, Y., Tanaka, N., Kakudo, M., Wada, K., & Matsubara, H. (1978) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a132293 · Cited by 50
Proline for alanine substitutions in the C-peptide helix of ribonuclease A
Strehlow, K. G., Robertson, A. D., & Baldwin, R. L. (1991) · Biochemistry · doi:10.1021/bi00237a026 · Cited by 48
Periodic properties of proton conformational shifts in isolated protein helices
Jiménez, M. A., Blanco, F. J., Rico, M., Santoro, J., Herranz, J. F., & NIETO, J. L. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17017.x · Cited by 48
Local effect of glycine substitution in a model helical peptide
Lyu, P. C., Wang, P. C., Liff, M. I., & Kallenbach, N. R. (1991) · Journal of the American Chemical Society · doi:10.1021/ja00009a052 · Cited by 32
Characterization of a synthetic calmodulin-binding peptide derived from Bacillus anthracis adenylate cyclase.
Munier‐Lehmann, H., Blanco, F. J., Prêcheur, B., Diesis, É., Nieto, J. L., Craescu, C. T., & Bârzu, O. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53908-9 · Cited by 32
1H‐NMR assignment and folding of the isolated ribonuclease 21–42 fragment
Jiménez, M. A., Rico, M., Herranz, J. F., Santoro, J., & NIETO, J. L. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14171.x · Cited by 31
Kinematics and thermodynamics of a folding heteropolymer.
Fukugita, M., Lancaster, D., & Mitchard, M. G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.13.6365 · Cited by 31
Secondary structure formation and stability
Ptitsyn, O. B. (1992) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(92)90170-c · Cited by 25
Conformational properties of the isolated 1–23 fragment of human hemoglobin α-chain
̃a, M. C. P., Rico, M., Jiménez, M. A., Herranz, J. F., Santoro, J., & Nieto, J. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90229-4 · Cited by 24
Position effect on apparent helical propensities in the C-peptide helix
Fairman, R., Armstrong, K. M., Shoemaker, K. R., York, E. J., Stewart, J. M., & Baldwin, R. L. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)80133-f · Cited by 22
Stabilization of α-Helix in C-Terminal Fragments of Neuropeptide Y
Yumoto, N., Murase, S., Hattori, T., Yamamoto, H., Tatsu, Y., & Yoshikawa, S. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.2420 · Cited by 22
A molecular thermodynamic approach to predict the secondary structure of homopolypeptides in aqueous systems
Chen, C., Zhu, Y., King, J. W., & Evans, L. B. (1992) · Biopolymers · doi:10.1002/bip.360321011 · Cited by 22
The homologous angiogenin and ribonuclease N-terminal fragments fold into very similar helices when isolated
Blanco, F. J., Jiménez, M. A., Rico, M., Santoro, J., Herranz, J. F., & Nieto, J. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91902-3 · Cited by 14
The contribution of helical potential to the in vitro receptor binding activity of a neuropeptide Y N‐terminal deletion fragment
Doughty, M. B., & Hu, L. (1993) · Biopolymers · doi:10.1002/bip.360330806 · Cited by 14
Conformations in solution of angiotensin II, and its 1–7 and 1–6 fragments
Cushman, J. A., Mishra, P. K., Bothner‐By, A. A., & Khosla, M. S. (1992) · Biopolymers · doi:10.1002/bip.360320905 · Cited by 12
Secondary-structure formation and stability
Ptitsyn, O. B. (1992) · Current Biology · doi:10.1016/0960-9822(92)90211-r · Cited by 12
Single‐residue substitution in homopolypeptides: Perturbative helix–coil theory at a single site
Qian, H. (1993) · Biopolymers · doi:10.1002/bip.360331010 · Cited by 11
NMR and circular dichroic studies on the solution conformation of a synthetic peptide derived from the calmodulin‐binding domain of Bordetella pertussis adenylate cyclase
PRÊHEUR, B., Siffert, O., Bârzu, O., & Craescu, C. T. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15786.x · Cited by 11
14.beta.-(Bromoacetamido)morphine irreversibly labels .mu. opioid receptors in rat brain membranes
Bidlack, J. M., Frey, D. K., Seyed‐Mozaffari, A., & Archer, S. (1989) · Biochemistry · doi:10.1021/bi00436a031 · Cited by 9
Conformation of uteroglobin fragments
Mammi, S., Foffani, M. T., Improta, S., Tessari, M., Schievano, E., & Peggion, E. (1992) · Biopolymers · doi:10.1002/bip.360320408 · Cited by 8
Preferred Local Conformations of Peptides comprising the Entire Sequence of Bovine Pancreatic Trypsin Inhibitor (BPTI) and their Roles in Protein Folding
Kemmink, J., & Creighton, T. E. (1994) · Springer eBooks · doi:10.1007/978-3-642-78846-8_14 · Cited by 4
Papel de los giros beta en el plegamiento de proteínas : estudio por resonancia magnética nuclear
Gutiérrez, F. J. B. (2012) · Dialnet (Universidad de la Rioja) · Cited by 1

Research works printed but not linked: 3

Peña M.C., 1989, Biochem. biophys. Acta., 957, 380
Dyson H.J., 1992, J. molec. Biol., 226, 817, 10.1016/0022-2836(92)90633-U · DOI
Chakrabarty, B.D., Doig, A.J. & Baldwin, R.L., Helix N-cap propensities in peptides parallel those found in proteins. Proc. natn. Acad. Sci. U.S.A. (in the press).

Sorted by citations

Interactions with Aromatic Rings in Chemical and Biological Recognition
Meyer, E. A., Castellano, R. K., & Diederich, F. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200390319 · Cited by 3,554
A Helix Propensity Scale Based on Experimental Studies of Peptides and Proteins
Pace, C. N., & Scholtz, J. M. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)77529-0 · Cited by 1,074
Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides
Best, R., & Hummer, G. (2009) · Journal of Physical Chemistry B · doi:10.1021/jp901540t · Cited by 826
Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins
Buck, M. (1998) · Quarterly Reviews of Biophysics · doi:10.1017/s003358359800345x · Cited by 829
A Survey of the Role of Noncovalent Sulfur Interactions in Drug Design
Beno, B. R., Yeung, K., Bartberger, M. D., Pennington, L. D., & Meanwell, N. A. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501853m · Cited by 791

See all 725

Authors: Muñoz, V., & Serrano, L.
Affiliations: European Molecular Biology Laboratory (DE)
Venue: Nature Structural & Molecular Biology
Publisher: Springer Science and Business Media LLC
Published: 1994-06
Volume: 1
Issue: 6
Pages: 399-409
ISSN: 1545-9985 (ISSN-L)
1545-9993
DOI: 10.1038/nsb0694-399
OpenAlex: W2083939457
Cited by: 721
References: 94
Citations by year: 2026: 12 · 2025: 9 · 2024: 17 · 2023: 19 · 2022: 19 · 2021: 16 · 2020: 20 · 2019: 14 · 2018: 26 · 2017: 20 · 2016: 15 · 2015: 20 · 2014: 31 · 2013: 29 · 2012: 23
FWCI: 8.52
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (unspecified)
Locations: Nature Structural & Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: helical peptides, alpha-helix stability, peptide folding, nuclear magnetic resonance
MeSH terms: Algorithms, Amino Acid Sequence, Circular Dichroism, Hydrogen Bonding, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Solutions, Ubiquitins, Protein Structure, Secondary, Protein Folding

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Elucidating the folding problem of helical peptides using empirical parameters

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks