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
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“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
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
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
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
