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Elucidating the folding problem of helical peptides using empirical parameters
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.
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“indeed, calculations of the percentage of helicity of the CC-Hex*-L24E monomer with Agadir114−118 show 13% helicity at pH 2 and 9% helicity at pH 8.5, with intermediate helicities in the pH range 2–8.5.”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [114]
Citations
Cites
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
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).
Cited by
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Items 501–600 of 725
Structural dissection of the C-terminal sterile alpha motif (SAM) of human p73
Neira, J. L. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.07.005 · Cited by 10
Engineering Folding Dynamics from Two-State to Downhill: Application to λ-Repressor
Carter, J. W., Baker, C. M., Best, R. B., & Sancho, D. D. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp405904g · Cited by 10
de Oliveira, O. V., de Moura, A. F., & Freitas, L. C. G. (2007) · Journal of Molecular Structure THEOCHEM · doi:10.1016/j.theochem.2006.12.039 · Cited by 10
Positional effects on helical Ala-based peptides.
Cheng, R. P., Girinath, P., Suzuki, Y., Kuo, H.-T., Hsu, H.-C., Wang, W.-R., Yang, P.-A., Gullickson, D., Wu, C.-H., Koyack, M. J., et al. (2010) · Biochemistry · doi:10.1021/bi101156j · Cited by 9
Muñoz, V., & Ramanathan, R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812577106 · Cited by 10
Self-citationHelix Forming Tendency of Valine Substituted Poly-Alanine: A Molecular Dynamics Investigation
Raman, S. S., Vijayaraj, R., Parthasarathi, R., & Subramanian, V. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp7119813 · Cited by 10
DNA bending by bHLH charge variants
McDonald, R. J., Kahn, J., & Maher, L. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl552 · Cited by 10
Ahmad, B., Vigliotta, I., Tatini, F., Campioni, S., Mannini, B., Winkelmann, J., Tiribilli, B., & Chiti, F. (2011) · Protein Engineering Design and Selection · doi:10.1093/protein/gzr018 · Cited by 10
Tensile Mechanics of α-Helical Polypeptides
Torabi, K., & Schatz, G. (2013) · Macromolecules · doi:10.1021/ma4015824 · Cited by 8
Compiani, M., Capriotti, E., & Casadio, R. (2004) · Physical Review E · doi:10.1103/physreve.69.051905 · Cited by 10
Low-density lipoprotein receptor-related protein 8 gene polymorphisms and dementia
Helbecque, N., Cottel, D., & Amouyel, P. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.05.024 · Cited by 10
Beyond the nearest‐neighbor Zimm–Bragg model for helix‐coil transition in peptides
Murza, A., & Kubelka, J. (2008) · Biopolymers · doi:10.1002/bip.21093 · Cited by 10
Guérois, R., Cordier-Ochsenbein, F., Neumann, J., Sanson, A., Baleux, F., & Huynh-Dinh, T. (1998) · Protein Science · doi:10.1002/pro.5560070703 · Cited by 9
Schütz, S., Bergsdorf, C., Hänni-Holzinger, S., Lingel, A., Renatus, M., Gossert, A. D., & Jahnke, W. (2024) · Biochemistry · doi:10.1021/acs.biochem.3c00608 · Cited by 9
Dinic, J., & Tirrell, M. (2024) · Biomacromolecules · doi:10.1021/acs.biomac.4c00002 · Cited by 9
Toward an improved structural model of the frog-skin antimicrobial peptide esculentin-1b(1-18).
Manzo, G., Sanna, R., Casu, M., Mignogna, G., Mangoni, M., Rinaldi, A., & Scorciapino, M. A. (2012) · Biopolymers · doi:10.1002/bip.22086 · Cited by 9
Imamura, H., Isogai, Y., & Kato, M. (2012) · Biochemistry · doi:10.1021/bi2019223 · Cited by 8
Helical Propensity in an Intrinsically Disordered Protein Accelerates Ligand Binding
Iešmantavičius, V., Dogan, J., Jemth, P., Teilum, K., & Kjærgaard, M. (2014) · Angewandte Chemie · doi:10.1002/ange.201307712 · Cited by 9
Luo, S., Wohl, S., Zheng, W., & Yang, S. (2023) · Biomolecules · doi:10.3390/biom13030530 · Cited by 10
Hornos, F., Feng, H., Rizzuti, B., Palomino‐Schätzlein, M., Wieczorek, D. F., Neira, J. L., & Jin, J. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.016012 · Cited by 9
Szczesniak, L. M., Bonzerato, C. G., Schulman, J. J., Bah, A., & Wojcikiewicz, R. J. H. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.03.047 · Cited by 9
Conlon, J. M., O'Harte, F. P. M., & Flatt, P. R. (2021) · Peptides · doi:10.1016/j.peptides.2021.170706 · Cited by 9
Joshi, R. G., Kulkarni, S., & Prabha, C. R. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.09.003 · Cited by 10
Graham, G. V., Conlon, J. M., Abdel‐Wahab, Y. H. A., & Flatt, P. R. (2018) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2018.10.011 · Cited by 9
Reddy, C. N., Manzar, N., Ateeq, B., & Sankararamakrishnan, R. (2020) · Biochemistry · doi:10.1021/acs.biochem.0c00661 · Cited by 9
Frère‐Gallois, V., Krebs, D. L., Scala, D., Troalen, F., & Fermandjian, S. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00142.x · Cited by 9
Watanabe, M., Kobashigawa, Y., Aizawa, T., Demura, M., & Nitta, K. (2004) · The Protein Journal · doi:10.1023/b:jopc.0000032653.30096.41 · Cited by 9
Corneal arcus: some morphology and applied pathophysiology.
Phillips, C. I., Tsukahara, S., & Gore, S. M. (1990) · PubMed · Cited by 9
Solid-state CD and peptide helical screw sense
Formaggio, F., Crisma, M., Toniolo, C., & Kamphuis, J. (1998) · Biopolymers · doi:10.1002/(sici)1097-0282(199603)38:3 · Cited by 27
Toiron, C., López, J. A., Rivas, G., Andreu, D., Melero, J. A., & Bruix, M. (1998) · Biopolymers · doi:10.1002/(sici)1097-0282(199610)39:4 · Cited by 15
Huang, S., Hu, M. Y., Lu, L., Kuang, Z., Heng, Y., Xu, L., Liang, X., Qiu, M., & Pan, X. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.07.017 · Cited by 8
Natarajan, L., Sciscio, M. L. D., Nardi, A. N., Sekhar, A., Giudice, A. D., D’Abramo, M., & Naganathan, A. N. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318855121 · Cited by 8
Laux, L., Janßen, M. A., & Thiele, C. M. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c09152 · Cited by 8
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Mosquera, J., Rodríguez, J., Vázquez, M. E., & Mascarenas, J. L. (2014) · ChemBioChem · doi:10.1002/cbic.201400079 · Cited by 8
Inhibition of talin-induced integrin activation by a double-hit stapled peptide
Gao, T., Cho, E.-A., Zhang, P., & Wu, J. (2023) · Structure · doi:10.1016/j.str.2023.05.016 · Cited by 7
Johal, A. R., Blackler, R., Alfaro, J., Schuman, B., Borisova, S., & Evans, S. (2014) · Glycobiology · doi:10.1093/glycob/cwt098 · Cited by 8
Neira, J. L., Hornos, F., Cozza, C., Cámara-Artigas, A., Abián, O., & Velázquez‐Campoy, A. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.12.017 · Cited by 8
Laursen, L. V., Čalyševa, J., Gibson, T. J., & Jemth, P. (2020) · Molecular Biology and Evolution · doi:10.1093/molbev/msaa198 · Cited by 9
Sequence Properties of an Intramolecular Interaction that Inhibits p53 DNA Binding
Gregory, E., & Daughdrill, G. W. (2022) · Biomolecules · doi:10.3390/biom12111558 · Cited by 8
A glutamine-based single α-helix scaffold to target globular proteins
Escobedo, A., Piccirillo, J., Aranda, J., Diercks, T., Mateos, B., Garcia‐Cabau, C., Sánchez‐Navarro, M., Topal, B., Biesaga, M., Staby, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34793-6 · Cited by 10
Rational peptide design for inhibition of the KIX–MLL interaction
Sato, N., Suetaka, S., Hayashi, Y., & Arai, M. (2023) · Scientific Reports · doi:10.1038/s41598-023-32848-2 · Cited by 8
Merkley, E., Bernard, B., & Daggett, V. (2008) · Biochemistry · doi:10.1021/bi701565b · Cited by 7
Folding initiation sites and protein folding.
Dadlez, M. (1999) · Acta Biochimica Polonica · doi:10.18388/abp.1999_4126 · Cited by 8
Ioannou, F., Leontidis, E., & Archontis, G. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp406231g · Cited by 8
Unfolding and inactivation of monomeric superoxide dismutase from E. coli by SDS
Bozzi, M., Battistoni, A., Sette, M., Melino, S., Rotilio, G., & Paci, M. (2001) · International Journal of Biological Macromolecules · doi:10.1016/s0141-8130(01)00146-5 · Cited by 8
Diffusion-collision model study of misfolding in a four-helix bundle protein.
Beck, C., Siemens, X., & Weaver, D. L. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75948-6 · Cited by 9
Kumaran, S., Datta, D., & Roy, R. P. (1997) · Protein Science · doi:10.1002/pro.5560061018 · Cited by 8
Myotubularin-related-protein-7 inhibits mutant (G12V) K-RAS by direct interaction
Weidner, P., Saar, D., Söhn, M., Schroeder, T., Yu, Y., Zöllner, F. G., Ponelies, N., Zhou, X., Zwicky, A., Rohrbacher, F. N., et al. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216783 · Cited by 7
Electrochemical and structural coupling of the naphthoquinone amino acid
Lichtenstein, B. R., Moorman, V. R., Cerda, J. F., Wand, A. J., & Dutton, P. L. (2011) · Chemical Communications · doi:10.1039/c2cc16968a · Cited by 7
Mechkarska, M., Coquet, L., Leprince, J., Jouenne, T., Vaudry, H., Michalak, K., Michalak, P., & Conlon, J. M. (2014) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2014.07.002 · Cited by 7
The temperature-dependent single-crystal Raman spectroscopy of a model dipeptide: l-Alanyl-l-alanine
Silva, J. G., Arruda, L. M., Pinheiro, G. S., Lima, C. L., Melo, F. E. A., Ayala, A. P., Fílho, J. M., & Freire, P. (2015) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2015.04.010 · Cited by 7
Rational design of a highly reactive dicysteine peptide tag for fluorogenic protein labelling.
Strmiskova, M., Tsao, K. K., & Keillor, J. (2018) · Organic and biomolecular chemistry · doi:10.1039/c8ob01417e · Cited by 4
Disorder for Dummies: Functional Mutagenesis of Transient Helical Segments in Disordered Proteins.
Daughdrill, G. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0524-0_1 · Cited by 8
Lee, J., Lee, H., & Kim, C. (2020) · New Journal of Chemistry · doi:10.1039/d0nj03409f · Cited by 7
Djajamuliadi, J., Ohgo, K., & Kumashiro, K. K. (2020) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c06811 · Cited by 6
Protposer: The web server that readily proposes protein stabilizing mutations with high PPV
García‐Cebollada, H., López, A., & Sancho, J. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.05.008 · Cited by 6
Absolute Net Charge and the Biological Activity of Oligopeptides
Parthasarathi, L., Devocelle, M., Søndergaard, C. R., Baran, I., O'Dushlaine, C., Davey, N. E., Edwards, R. J., Moran, N., Kenny, D., & Shields, D. (2006) · Journal of Chemical Information and Modeling · doi:10.1021/ci0600760 · Cited by 5
De novo design of stable α-helices.
Yakimov, A., Rychkov, G., & Petukhov, M. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-1486-9_1 · Cited by 5
Gaiser, R. A., Mangado, J. A., Mechkarska, M., Kaman, W. E., van Baarlen, P., Conlon, J. M., & Wells, J. M. (2019) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13569 · Cited by 7
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Ahmad, A., Rilla, K. J., Zou, J., Zhang, W., Pyykkö, I. V., Kinnunen, P. K. J., & Ranjan, S. K. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.120556 · Cited by 7
Pantic, J. M., Guilhaudis, L., Musale, V., Attoub, S., Lukić, M. L., Mechkarska, M., & Conlon, J. M. (2019) · Journal of Peptide Science · doi:10.1002/psc.3153 · Cited by 7
Condamine, E., Leprince, J., Suaudeau, C., Mayer, C., Davoust, D., Costentin, J., & Vaudry, H. (1999) · Peptides · doi:10.1016/s0196-9781(99)00074-1 · Cited by 7
Modulating the DNA Affinity of Elk-1 with Computationally Selected Mutations
Park, S., Boder, E. T., & Saven, J. G. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.12.062 · Cited by 7
Analysis of Disordered Proteins by Hydrogen Exchange Mass Spectrometry
Weis, D. D. (2016) · Wiley eBooks · doi:10.1002/9781118703748.ch17 · Cited by 7
The Folding Thermodynamics and Kinetics of Crambin Using an All-Atom Monte Carlo SimulationPreprint
Shimada, J., Kussell, E. L., & Shakhnovich, E. I. (2000) · arXiv (Cornell University) · doi:10.48550/arxiv.cond-mat/0011369 · Cited by 8
Mutational scan inferred binding energetics and structure in intrinsically disordered protein CcdA
Chandra, S., Manjunath, K., Asok, A., & Varadarajan, R. (2023) · Protein Science · doi:10.1002/pro.4580 · Cited by 7
Rejnowicz, E., Batchelor, M. R., Leen, E. N., Ahangar, M. S., Burgess, S. G., Richards, M. W., Kalverda, A. P., & Bayliss, R. W. (2024) · Biochemical Journal · doi:10.1042/bcj20240248 · Cited by 9
Sánchez‐Acosta, Y. A., Vargas, J. A. C., Quintero, K. J. R., Ordúz, S., & Camargo, O. (2020) · Reproduction in Domestic Animals · doi:10.1111/rda.13701 · Cited by 6
Jara, K. A., Loening, N. M., Reardon, P. N., Yu, Z., Woonnimani, P., Brooks, C., Vesely, C. H., & Barbar, E. J. (2022) · eLife · doi:10.7554/elife.80217 · Cited by 6
Structural stability studies in adhesion molecules—role of cation–π interactions
Sophiya, K., & Anbarasu, A. (2010) · PROTOPLASMA · doi:10.1007/s00709-010-0224-7 · Cited by 6
What Determines the Activity of Antimicrobial and Cytolytic Peptides in Model Membranes
Almeida, P., Clark, K. S., Svetlovics, J., McKeown, A. N., & Huskins, L. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.11.512
Treviño, M. Á., Rodríguez‐Rodríguez, M., Correas, I., Marcilla, M., Albar, J. P., Rico, M., Jiménez, M. A., & Bruix, M. (2010) · BMC Biochemistry · doi:10.1186/1471-2091-11-7 · Cited by 6
Robustelli, J., & Baumgart, T. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183660 · Cited by 6
Mitochondrial DNA Changes in Respiratory Complex I Genes in Brain Gliomas
Kozakiewicz, P., Grzybowska‐Szatkowska, L., Ciesielka, M., Całka, P., Osuchowski, J., Szmygin, P., Jarosz, B., Ostrowska-Leśko, M., Dudka, J., Tkaczyk‐Wlizło, A., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11041183 · Cited by 6
Haddad, H., Mejri, R., ARAUJO, A. R. D., & Zaïri, A. (2024) · Pharmaceuticals · doi:10.3390/ph17020171 · Cited by 6
Duan, M., Liu, H., Li, M., & Huo, S. (2015) · The Journal of Chemical Physics · doi:10.1063/1.4931921 · Cited by 5
Glyakina, A. V., Pereyaslavets, L. B., & Galzitskaya, O. V. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24301 · Cited by 6
Lee, J., Oh, E., Joo, Y.-E., Kim, H. G., Park, H. J., & Kim, C. (2020) · New Journal of Chemistry · doi:10.1039/d0nj04608f · Cited by 6
A structural study of model peptides derived from HIV-1 integrase central domain.
Maroun, R., Zargarian, L., Stocklin, R., Troalen, F., Jankowski, C., & Fermandjian, S. (2005) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.2093 · Cited by 5
Mutational Analysis and Structure Predictions
Blüthner, M., Koch, J., & Mähler, M. (2002) · Springer eBooks · doi:10.1007/978-3-662-09229-3_9 · Cited by 6
López‐Hernández, E., & Serrano, L. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340220405 · Cited by 6
Self-citationHRMAS NMR observation of β‐sheet secondary structure on a water swollen solid support
Rousselot‐Pailley, P., Boutillon, C., Wieruszeski, J., & Lippens, G. M. (2003) · Journal of Peptide Science · doi:10.1002/psc.431 · Cited by 6
Suárez, I. P., Gauto, D. F., Hails, G., Mascali, F. C., Crespo, R., Zhao, L., Wang, J., & Rasia, R. M. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp07908g · Cited by 5
Toxoplasma Gondii Importin α Shows Weak Auto-Inhibition
Bhambid, M., Dey, V., Walunj, S., & Patankar, S. (2023) · The Protein Journal · doi:10.1007/s10930-023-10128-2 · Cited by 5
Correlating disordered activation domain ensembles with gene expression levels
Flores, E., Camacho, A. R., Cuevas-Zepeda, E., McCoy, M., Yu, F., Staller, M. V., & Sukenik, S. (2025) · Biophysical Reports · doi:10.1016/j.bpr.2024.100195 · Cited by 6
Design of affinity peptides from natural protein ligands: A study of the cardiac troponin complex
Chandra, D., Sankalia, N., Arcibal, I. G., Banta, S., Cropek, D., & Karande, P. (2014) · Biopolymers · doi:10.1002/bip.22436 · Cited by 5
Side-chain–side-chain interactions and stability of the helical state
Zangi, R. (2014) · Physical Review E · doi:10.1103/physreve.89.012723 · Cited by 5
Transition states in protein folding
Weikl, T. (2009) · Communications in Computational Physics · doi:10.4208/cicp.2009.08.202 · Cited by 12
Vymětal, J., Bathula, S. R., Černý, J., Chaloupková, R., Žı́dek, L., Sklenář, V., & Vondrášek, J. (2014) · Protein Engineering Design and Selection · doi:10.1093/protein/gzu046 · Cited by 5
Structural and mechanistic insights into EchAMP: A antimicrobial protein from the Echidna milk.
Kumar, A., Parveen, S., Sharma, I., Pathak, H., Deshmukh, M., Sharp, J., & Kumar, S. (2019) · Biochimica et Biophysica Acta - Biomembranes · doi:10.1016/j.bbamem.2019.03.020 · Cited by 4
Incorporating Polarizability of Backbone Hydrogen Bonds Improved Folding of Short α-Helical Peptides
Zhang, D., Lazim, R., & Yip, Y. M. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.10.020 · Cited by 5
Kennedy, J. A., Syed, S., & Schmidt, K. H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145466 · Cited by 5
Krebs, D., Dahmani, B., Monnot, M., Mauffret, O., Troalen, F., & Fermandjian, S. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.t01-1-00699.x · Cited by 5
Fernández, I., Ubach, J., Fuxreiter, M., Andreu, J. M., Andreu, D., & Pons, M. (1996) · Chemistry - A European Journal · doi:10.1002/chem.19960020717 · Cited by 5
Highly polar environments catalyze the unfolding of PrPC helix 1
Lingenheil, M., Denschlag, R., & Tavan, P. (2010) · European Biophysics Journal · doi:10.1007/s00249-009-0570-6 · Cited by 5
A generic expression system to produce proteins that co-assemble with alkane thiol SAM
Lakey, J. H. (2008) · International Journal of Nanomedicine · doi:10.2147/ijn.s2655 · Cited by 5
Ziegler, J., & Schwarzinger, S. (2006) · J. Comput. Aided Mol. Des. · doi:10.1007/s10822-006-9035-5 · Cited by 7
Mizuguchi, M., Matsuura, A., Nabeshima, Y., Masaki, K., Watanabe, M., Aizawa, T., Demura, M., Nitta, K., Mori, Y., Shinoda, H., et al. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20640 · Cited by 5
Learning effective amino acid interactions through iterative stochastic techniques
Micheletti, C., Seno, F., Banavar, J. R., & Maritan, A. (2001) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20010215)42:3 · Cited by 55
Roberts, S., Harmon, T. S., Schaal, J. L., Miao, V. N., Li, K., Hunt, A. C., Wen, Y., Oas, T. G., Collier, J. H., Pappu, R. V., et al. (2018) · Nature Materials · doi:10.1038/s41563-018-0233-z · Cited by 8
Metadata
- Authors
- Muñoz, V., & Serrano, L.
- Affiliations
- European Molecular Biology Laboratory (DE)
- Venue
- Nature Structural & Molecular Biology
- Published
- 1994-06
- Volume
- 1
- Issue
- 6
- Pages
- 399-409
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- 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
- 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
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