The Protein Folding Problem: The Role of Theory

被引：67

作者：

Nassar, Roy ^{[1
,2
]}

Dignon, Gregory L. ^{[1
]}

Razban, Rostam M. ^{[1
]}

Dill, Ken A. ^{[1
,2
,3
]}

机构：

[1] SUNY Stony Brook, Laufer Ctr Phys & Quantitat Biol, Stony Brook, NY 11794 USA

[2] SUNY Stony Brook, Dept Chem, Stony Brook, NY 11794 USA

[3] SUNY Stony Brook, Dept Phys & Astron, Stony Brook, NY 11794 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2021年 / 433卷 / 20期

关键词：

protein folding theory; statistical mechanics; disordered proteins; protein aggregation; coarse-grained modeling; LIQUID PHASE-SEPARATION; INTRINSICALLY DISORDERED PROTEINS; REVERSIBLE SELF-ASSOCIATION; HIGHLY EXPRESSED PROTEINS; ALPHA-HELIX FORMATION; SIMPLE-MODEL; NATIVE-STATE; RANDOM-COIL; X-RAY; STATISTICAL-MECHANICS;

D O I：

10.1016/j.jmb.2021.167126

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2021 Elsevier Ltd. All rights reserved.

引用

页数：24

共 50 条

[41] φ values in protein-folding kinetics have energetic and structural components [J].

Merlo, C ;

Dill, KA ;

Weikl, TR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (29) :10171-10175

[42] Understanding protein non-folding [J].

Uversky, Vladimir N. ;

Dunker, A. Keith .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2010, 1804 (06) :1231-1264

[43] Heterogeneity in Protein Folding and Unfolding Reactions [J].

Bhatia, Sandhya ;

Udgaonkar, Jayant B. .

CHEMICAL REVIEWS, 2022, 122 (09) :8911-8935

[44] Unraveling the Mysteries of Protein Folding and Misfolding [J].

Ecroyd, Heath ;

Carver, John A. .

IUBMB LIFE, 2008, 60 (12) :769-774

[45] The role of water in the primary nucleation of protein amyloid aggregation [J].

Camino, Jose D. ;

Gracia, Pablo ;

Cremades, Nunilo .

BIOPHYSICAL CHEMISTRY, 2021, 269

[46] Protein Folding and the Order/Disorder Paradox [J].

Kulkarni, Prakash ;

Rajagopalan, Krithika ;

Yeater, David ;

Getzenberg, Robert H. .

JOURNAL OF CELLULAR BIOCHEMISTRY, 2011, 112 (07) :1949-1952

[47] Protein folding, cellular stress and cancer [J].

Aranda-Anzaldo, Armando ;

Dent, Myrna A. R. ;

Segura-Anaya, Edith ;

Martinez-Gomez, Alejandro .

PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 2024, 191 :40-57

[48] Quantum intelligence on protein folding pathways [J].

Mao, Wen-Wen ;

Lv, Li-Hua ;

Ji, Yong-Yun ;

Li, You-Quan .

CHINESE PHYSICS B, 2020, 29 (01)

[49] PHENOTYPIC TRAITS AND REGULATORY ROLE OF RNA FOLDING IN MOLECULAR-SELECTION [J].

FERNANDEZ, A .

ZEITSCHRIFT FUR NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES, 1991, 46 (7-8) :656-662

[50] Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E-coli [J].

Hesterkamp, T ;

Bukau, B .

EMBO JOURNAL, 1998, 17 (16) :4818-4828

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