Charge Distribution Patterns of IA3 Impact Conformational Expansion and Hydration Diffusivity of the Disordered Ensemble
Author:
Affiliation:
1. Department of Chemistry, University of Florida, P.O. Box 117200, Gainesville, Florida 32611, United States
2. Materials Research Laboratory, University of California, Santa Barbara, California 93106, United States
Funder
Division of Molecular and Cellular Biosciences
NIH National Institutes of Health
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.3c06170
Reference83 articles.
1. Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins
2. Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues
3. Intrinsically unstructured proteins and their functions
4. CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins
5. Net charge per residue modulates conformational ensembles of intrinsically disordered proteins
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