Competition between Reversible Aggregation and Loop Formation in Denatured Iso-1-cytochrome c
Author:
Affiliation:
1. Department of Chemistry and Biochemistry and Center for Biomolecular Structure and Dynamics, The University of Montana, Missoula, Montana 59812, and Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi801977j
Reference35 articles.
1. Alternative Explanations for “Multistate” Kinetics in Protein Folding: Transient Aggregation and Changing Transition-State Ensembles
2. Intermolecular aggregations are responsible for the slow kinetics observed in the folding of cytochrome c at neutral pH 1 1Edited by P. E. Wright
3. Binary and Ternary Aggregation within Tethered Protein Constructs
4. Protein folding and misfolding
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