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Cited by 312

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Folding of Polypeptide Chains in Proteins: A Proposed Mechanism for Folding

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Lewis, Peter N., Momany, Frank A., Scheraga, Harold A.·1971·Proceedings of the National Academy of Sciences

Abstract

A mechanism is proposed for the folding of protein chains. On the basis of short-range interactions, certain aminoacid sequences have a high propensity to be, say, α-helical. However, these short helical (or other ordered) regions can be stabilized only by long-range interactions arising from the proximity of two such ordered regions. These regions are brought near each other by the directing influence of certain other aminoacid sequences that have a high probability of forming β-bends or variants thereof, also on the basis of short-range interactions. An analysis is made of the tendency of various amino acids to occur in β-bends, and it is possible to predict the regions of a chain in which a β-bend will occur with a high degree of reliability.

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Metadata

Authors
Lewis, P. N., Momany, F. A., & Scheraga, H. A.
Venue
Proceedings of the National Academy of Sciences
Published
1971-09
Volume
68
Issue
9
Pages
2293-2297
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2018645145
Cited by
312
References
0
FWCI
5.50
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Folding of Polypeptide Chains in Proteins: A Proposed Mechanism for Folding. https://app.cochat.ai/papers/10.1073/pnas.68.9.2293
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Lewis, P. N., Momany, F. A., & Scheraga, H. A. (1971). Folding of Polypeptide Chains in Proteins: A Proposed Mechanism for Folding. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.68.9.2293

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.