New Insights into Protein (Un)Folding Dynamics.
J Phys Chem Lett
; 6(6): 1082-6, 2015 Mar 19.
Article
in En
| MEDLINE
| ID: mdl-25866611
ABSTRACT
A fundamental open problem in biophysics is how the folded structure of the main chain (MC) of a protein is determined by the physics of the interactions between the side chains (SCs). All-atom molecular dynamics simulations of a model protein (Trp-cage) revealed that strong correlations between the motions of the SCs and the MC occur transiently at 380 K in unfolded segments of the protein and during the simulations of the whole amino-acid sequence at 450 K. The high correlation between the SC and MC fluctuations is a fundamental property of the unfolded state and is also relevant to unstructured proteins as intrinsically disordered proteins (IDPs), for which new reaction coordinates are introduced. The presented findings may open a new door as to how functions of IDPs are related to conformations, which play a crucial role in neurodegenerative diseases.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptides
/
Proteins
/
Protein Folding
Type of study:
Prognostic_studies
Limits:
Humans
Language:
En
Journal:
J Phys Chem Lett
Year:
2015
Document type:
Article