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Kinetics of protein unfolding at interfaces.

Authors
  • Yano, Yohko F
Type
Published Article
Journal
Journal of Physics Condensed Matter
Publisher
IOP Publishing
Publication Date
Dec 19, 2012
Volume
24
Issue
50
Pages
503101–503101
Identifiers
DOI: 10.1088/0953-8984/24/50/503101
PMID: 23164927
Source
Medline
License
Unknown

Abstract

The conformation of protein molecules is determined by a balance of various forces, including van der Waals attraction, electrostatic interaction, hydrogen bonding, and conformational entropy. When protein molecules encounter an interface, they are often adsorbed on the interface. The conformation of an adsorbed protein molecule strongly depends on the interaction between the protein and the interface. Recent time-resolved investigations have revealed that protein conformation changes during the adsorption process due to the protein-protein interaction increasing with increasing interface coverage. External conditions also affect the protein conformation. This review considers recent dynamic observations of protein adsorption at various interfaces and their implications for the kinetics of protein unfolding at interfaces.

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