Sequence of Events during Peptide Unbinding from RNase S: A Complete Experimental Description.
J Phys Chem Lett
; 12(21): 5201-5207, 2021 Jun 03.
Article
em En
| MEDLINE
| ID: mdl-34038133
ABSTRACT
The phototriggered unbinding of the intrinsically disordered S-peptide from the RNase S complex is studied with the help of transient IR spectroscopy, covering a wide range of time scales from 100 ps to 10 ms. To that end, an azobenzene moiety has been linked to the S-peptide in a way that its helicity is disrupted by light, thereby initiating its complete unbinding. The full sequence of events is observed, starting from unfolding of the helical structure of the S-peptide on a 20 ns time scale while still being in the binding pocket of the S-protein, S-peptide unbinding after 300 µs, and the structural response of the S-protein after 3 ms. With regard to the S-peptide dynamics, the binding mechanism can be classified as an induced fit, while the structural response of the S-protein is better described as conformational selection.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Ribonucleases
/
Proteínas Intrinsicamente Desordenadas
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article