Thermodynamics of Protein Self-Association and Unfolding. The Case of Apolipoprotein A-I
Author:
Affiliation:
1. Division of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland
2. Pharmaceutical Research, F. Hoffman-La Roche Ltd., CH-4070 Basel, Switzerland
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi2013799
Reference41 articles.
1. Structure and function of apolipoprotein A-I and high-density lipoprotein
2. Apolipoprotein A-I: structure–function relationships
3. Crystal Structure of C-terminal Truncated Apolipoprotein A-I Reveals the Assembly of High Density Lipoprotein (HDL) by Dimerization
4. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
5. Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state.
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