Residue-Specific Description of Non-Native Transient Structures in the Ensemble of Acid-Denatured Structures of the All-β Protein c-src SH3
Author:
Affiliation:
1. Structure Biology and NMR Laboratory, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi902125j
Reference42 articles.
1. NMR Structural and Dynamic Characterization of the Acid-Unfolded State of Apomyoglobin Provides Insights into the Early Events in Protein Folding,
2. Transient Structure Formation in Unfolded Acyl-coenzyme A-binding Protein Observed by Site-directed Spin Labelling
3. Characterisation of the Conformational Properties of Urea-unfolded Im7: Implications for the Early Stages of Protein Folding
4. NMR characterization of residual structure in the denatured state of protein L
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