The Protein Folding Problem: The Role of Theory
| Autor: | Roy Nassar, Rostam M. Razban, Ken A. Dill, Gregory L. Dignon |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Protein Folding Biochemistry & Molecular Biology Protein Conformation protein folding theory Bioengineering coarse-grained modeling Protein aggregation Microbiology Article protein aggregation Protein Aggregates Medicinal and Biomolecular Chemistry Chain (algebraic topology) Structural Biology Models Animals Humans Statistical physics Molecular Biology Conformational ensembles Randomness Physical science Proteins Molecular Statistical mechanics Intrinsically Disordered Proteins Order (biology) Protein folding statistical mechanics Biochemistry and Cell Biology disordered proteins |
| Zdroj: | Journal of molecular biology, vol 433, iss 20 J Mol Biol |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|