Residual Structure in the Denatured State of the Fast-Folding UBA(1) Domain from the Human DNA Excision Repair Protein HHR23A
Author:
Affiliation:
1. Department of Chemistry & Biochemistry, University of Montana, Missoula, Montana 59812, United States
2. Center for Biomolecular Structure & Dynamics, University of Montana, Missoula, Montana 59812, United States
Funder
Division of Chemistry
Division of Molecular and Cellular Biosciences
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00011
Reference128 articles.
1. Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding
2. 3.5 Characterization of the Denatured State
3. Atomic-level characterization of disordered protein ensembles
4. Methods in Molecular Biology;Eliezer D.,2007
5. Molecular Hinges in Protein Folding: the Urea-Denatured State of Apomyoglobin†
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