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Influence of proline residues on protein conformation
Abstract
To study the influence of proline residues on three-dimensional structure, an analysis has been made of all proline residues and their local conformations extracted from the Brookhaven Protein Data bank. We have considered the conformation of the proline itself, the relative occurrence of cis and trans peptides preceding proline residues, the influence of proline on the conformation of the preceding residue and the conformations of various proline patterns (Pro-Pro, Pro-X-Pro, etc.). The results highlight the unique role of proline in determining local conformation.
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“a very finely balanced energy difference with about only one in 15 prolines in protein structures adopting the cis form50.”
From Critical assessment of methods of protein structure prediction (CASP)—Round XIV (2021) · cites this paper as [50]
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Metadata
- Authors
- MacArthur, M. W., & Thornton, J. M.
- Affiliations
- University College London (GB)
- ORCID
- Thornton, Janet M.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1991-03
- Volume
- 218
- Issue
- 2
- Pages
- 397-412
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2047572594
- Cited by
- 1,189
- References
- 29
- Citations by year
- 2026: 32 · 2025: 34 · 2024: 34 · 2023: 21 · 2022: 32 · 2021: 36 · 2020: 33 · 2019: 35 · 2018: 31 · 2017: 27 · 2016: 37 · 2015: 37 · 2014: 32 · 2013: 45 · 2012: 35
- FWCI
- 10.97
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of 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 › Structural Biology › Enzyme Structure and Function
- Keywords
- proline residues, protein conformation, local conformation, cis-trans isomerization, peptide backbone conformation, protein structure, Protein Data Bank
- MeSH terms
- Amino Acid Sequence, Crystallization, Glycine, Hydrogen Bonding, Molecular Sequence Data, Proline, Protein Conformation, Databases, Factual
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 ›
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