Solvation in protein (un)folding of melittin tetramer-monomer transition

Protein structural integrity and flexibility are intimately tied to solvation. Here, we examine the effect that changes in bulk and local solvent properties have on protein structure and stability. We observe the change in solvation of an unfolding of the protein model, melittin, in the presence of...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2009-08, Vol.106 (31), p.12593-12598
Main Authors: Othon, Christina M, Kwon, Oh-Hoon, Lin, Milo M, Zewail, Ahmed H
Format: Article
Language:English
Subjects:
Alcohols
Anisotropy
Biochemistry
Biological Sciences
Biopolymers - chemistry
Fluorescence
Melitten - chemistry
Molecules
Monomers
Peptides
Physical Sciences
Protein Folding
Protein Structure, Secondary
Proteins
Rotation
Solution chemistry
Solvation
Solvents
Solvents - chemistry
Spectrometry, Fluorescence
Time constants
Trifluoroethanol - chemistry
Viscosity
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Protein structural integrity and flexibility are intimately tied to solvation. Here, we examine the effect that changes in bulk and local solvent properties have on protein structure and stability. We observe the change in solvation of an unfolding of the protein model, melittin, in the presence of a denaturant, trifluoroethanol. The peptide system displays a well defined transition in that the tetramer unfolds without disrupting the secondary or tertiary structure. In the absence of local structural perturbation, we are able to reveal exclusively the role of solvation dynamics in protein structure stabilization and the (un)folding pathway. A sudden retardation in solvent dynamics, which is coupled to the change in protein structure, is observed at a critical trifluoroethanol concentration. The large amplitude conformational changes are regulated by the local solvent hydrophobicity and bulk solvent viscosity.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0905967106