Rethinking the protein folding problem from a new perspective.
Eur Biophys J
; 52(3): 189-193, 2023 Apr.
Article
em En
| MEDLINE
| ID: mdl-37165178
One of the main concerns of Anfinsen was to reveal the connection between the amino-acid sequence and their biologically active conformation. This search gave rise to two crucial questions in structural biology, namely, why the proteins fold and how a sequence encodes its folding. As to the why, he proposes a plausible answer, namely, the thermodynamic hypothesis. As to the how, this remains an unsolved challenge. Consequently, the protein folding problem is examined here from a new perspective, namely, as an 'analytic whole'. Conceiving the protein folding in this way enabled us to (i) examine in detail why the force-field-based approaches have failed, among other purposes, in their ability to predict the three-dimensional structure of a protein accurately; (ii) propose how to redefine them to prevent these shortcomings, and (iii) conjecture on the origin of the state-of-the-art numerical-methods success to predict the tridimensional structure of proteins accurately.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Dobramento de Proteína
Idioma:
En
Revista:
Eur Biophys J
Assunto da revista:
BIOFISICA
Ano de publicação:
2023
Tipo de documento:
Article
País de afiliação:
Argentina
País de publicação:
Alemanha