A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution

Autor:	Alan R. Fersht, Dmitry M. Korzhnev, Lewis E. Kay, Wiktor Banachewicz, Tomasz L. Religa
Rok vydání:	2010
Předmět:	Folding (chemistry) Crystallography Multidisciplinary Protein structure Chemistry Chemical physics Chemical shift Relaxation (NMR) Kinetics Native state Intermediate state Protein folding
Zdroj:	Science. 329:1312-1316
ISSN:	1095-9203 0036-8075
Popis:	Transient Protein Conformations Transient conformations are important to protein function; however, detecting and characterizing these states is technically challenging. Korzhnev et al. (p. 1312 ; see the Perspective by Al-Hashimi ) combined recently developed methods to determine the three-dimensional atomic-resolution structure of a transient intermediate of a four-helix bundle protein domain. The intermediate formed rapidly but, owing to structural peculiarities, slowly rearranged into its native state. The methods can be applied not only to folding intermediates but also to excited states important for protein function.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::18e114ec61aaea2e70b2cf1b7bdec131 https://doi.org/10.1126/science.1191723 Zobrazit plný text záznamu Plný text ve formátu PDF