The Protein Folding Problem: The Role of Theory. Issue 20 (1st October 2021)

• Record Type: Journal Article
• Authors: Nassar, Roy; Dignon, Gregory L.; Razban, Rostam M.; Dill, Ken A.
• Is Part Of: Journal of molecular biology. Volume 433:Issue 20(2021)
• Publication Date: 2021-10-01
• Subjects: protein folding theory -- statistical mechanics -- disordered proteins -- protein aggregation -- coarse-grained modeling; Molecular biology -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Bacteriology -- Periodicals; Molecular Biology -- Periodicals; Biochemistry -- Periodicals; Biologie moléculaire -- Périodiques; Biologie -- Périodiques; Biochimie -- Périodiques; Moleculaire biologie; Biochemistry; Biology; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.jmb.2021.167126
• Languages: English
• ISSNs: 0022-2836

Abstract

Graphical abstract: Highlights: The protein folding problem consisted of a set of core conceptual questions. The questions were of theoretical physical and chemical nature. Theory solved the problems about stabilities and rates using statistical mechanics. Recent theories investigated the concurrent interactions of multiple proteins. Abstract: 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.