Unusual domain movement in a multidomain protein in the presence of macromolecular crowders
Author:
Affiliation:
1. Department of Chemistry
2. Indian Institute of Technology Delhi
3. New Delhi 110016
4. India
Abstract
FRET-based distance changes between domains I and II of HSA reveal significant differences in the manner in which dextran based macromolecular crowding agents influence the serum protein.
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2015/CP/C5CP02674A
Reference43 articles.
1. Effects of macromolecular crowding on protein folding and aggregation
2. Models for Excluded Volume Interaction between an Unfolded Protein and Rigid Macromolecular Cosolutes: Macromolecular Crowding and Protein Stability Revisited
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4. Macromolecular Crowding: Biochemical, Biophysical, and Physiological Consequences
5. Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences
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