Understanding a protein fold: The physics, chemistry, and biology of α-helical coiled coils.

Biology Physics Protein Conformation, alpha-Helical Protein Domains Protein Folding Proteins / chemistry

coiled coil peptide assembly protein design quaternary structure structural biology α helix

Journal

The Journal of biological chemistry

ISSN: 1083-351X

Titre abrégé: J Biol Chem

Pays: United States

ID NLM: 2985121R

Informations de publication

Date de publication:
04 2023

Historique:

received: 03 01 2023

revised: 25 02 2023

accepted: 27 02 2023

medline: 28 4 2023

pubmed: 6 3 2023

entrez: 5 3 2023

Statut: ppublish

Résumé

Protein science is being transformed by powerful computational methods for structure prediction and design: AlphaFold2 can predict many natural protein structures from sequence, and other AI methods are enabling the de novo design of new structures. This raises a question: how much do we understand the underlying sequence-to-structure/function relationships being captured by these methods? This perspective presents our current understanding of one class of protein assembly, the α-helical coiled coils. At first sight, these are straightforward: sequence repeats of hydrophobic (h) and polar (p) residues, (hpphppp)

Identifiants

DOI: 10.1016/j.jbc.2023.104579 PMID: 36871758 PMC: PMC10124910

pubmed: 36871758

pii: S0021-9258(23)00221-1

doi: 10.1016/j.jbc.2023.104579

pmc: PMC10124910

pii:

doi:

Substances chimiques

Proteins 0

Types de publication

Journal Article Review Research Support, Non-U.S. Gov't

Langues

eng