The Partially Folded Homodimeric Intermediate of Escherichia coli Aspartate Aminotransferase Contains a “Molten Interface” Structure
Author:
Affiliation:
1. Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3206
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi801431x
Reference58 articles.
1. The Unfolding Pathway for Apo Escherichia coli Aspartate Aminotransferase Is Dependent on the Choice of Denaturant
2. Cofactor-Directed Reversible Denaturation Pathways: The Cofactor-Stabilized Escherichia coli Aspartate Aminotransferase Homodimer Unfolds through a Pathway That Differs from That of the Apoenzyme
3. Experimental assignment of the structure of the transition state for the association of barnase and barstar11Edited by B. Honig
4. Folding intermediates of wild-type and mutants of barnase. II. correlation of changes in equilibrium amide exchange kinetics with the population of the folding intermediate
5. Folding intermediates of wild-type and mutants of barnase. I. use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium
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1. Engineering homooligomeric proteins to detect weak intersite allosteric communication: Aminotransferases, a case study;Protein Science;2011-11-01
2. Biophysical characterization of Entamoeba histolytica phosphoserine aminotransferase (EhPSAT): role of cofactor and domains in stability and subunit assembly;European Biophysics Journal;2010-12-16
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