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Tytuł pozycji:

The Protein Folding Problem: The Role of Theory.

Tytuł:
The Protein Folding Problem: The Role of Theory.
Autorzy:
Nassar R; Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY, USA; Department of Chemistry, Stony Brook University, Stony Brook, NY, USA.
Dignon GL; Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY, USA.
Razban RM; Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY, USA.
Dill KA; Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY, USA; Department of Chemistry, Stony Brook University, Stony Brook, NY, USA; Department of Physics and Astronomy, Stony Brook University, Stony Brook, NY, USA. Electronic address: .
Źródło:
Journal of molecular biology [J Mol Biol] 2021 Oct 01; Vol. 433 (20), pp. 167126. Date of Electronic Publication: 2021 Jul 03.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Review
Język:
English
Imprint Name(s):
Publication: Amsterdam : Elsevier
Original Publication: 1959- : London : Academic Press
MeSH Terms:
Protein Folding*
Proteins/*chemistry
Animals ; Humans ; Intrinsically Disordered Proteins/chemistry ; Models, Molecular ; Protein Aggregates ; Protein Conformation
References:
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Grant Information:
RM1 GM135136 United States GM NIGMS NIH HHS
Contributed Indexing:
Keywords: coarse-grained modeling; disordered proteins; protein aggregation; protein folding theory; statistical mechanics
Substance Nomenclature:
0 (Intrinsically Disordered Proteins)
0 (Protein Aggregates)
0 (Proteins)
Entry Date(s):
Date Created: 20210705 Date Completed: 20211109 Latest Revision: 20240403
Update Code:
20240403
PubMed Central ID:
PMC8547331
DOI:
10.1016/j.jmb.2021.167126
PMID:
34224747
Czasopismo naukowe
The protein folding problem was first articulated as question of how order arose from disorder in proteins: How did the various native structures of proteins arise from interatomic driving forces encoded within their amino acid sequences, and how did they fold so fast? These matters have now been largely resolved by theory and statistical mechanics combined with experiments. There are general principles. Chain randomness is overcome by solvation-based codes. And in the needle-in-a-haystack metaphor, native states are found efficiently because protein haystacks (conformational ensembles) are funnel-shaped. Order-disorder theory has now grown to encompass a large swath of protein physical science across biology.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2021 Elsevier Ltd. All rights reserved.)

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