Influence of an Intrinsically Disordered Region on Protein Domains Revealed by NMR-Based Electrostatic Potential Measurements
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-1068, United States
Funder
Welch Foundation
Division of Molecular and Cellular Biosciences
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.4c03254
Reference31 articles.
1. Negatively Charged Disordered Regions are Prevalent and Functionally Important Across Proteomes
2. Genome-wide survey of D/E repeats in human proteins uncovers their instability and aids in identifying their role in the chromatin regulator ATAD2
3. Tail-Mediated Collapse of HMGB1 Is Dynamic and Occurs via Differential Binding of the Acidic Tail to the A and B Domains
4. Mapping Intramolecular Interactions between Domains in HMGB1 using a Tail-truncation Approach
5. Identification of Novel Domains within Sox-2 and Sox-11 Involved in Autoinhibition of DNA Binding and Partnership Specificity
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1. Gadolinium-Based NMR Spin Relaxation Measurements of Near-Surface Electrostatic Potentials of Biomolecules;Journal of the American Chemical Society;2024-07-19
2. Phosphorylation by Protein Kinase C Weakens DNA-Binding Affinity and Folding Stability of the HMGB1 Protein;Biochemistry;2024-06-25
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