Optical Spectroscopic Characterization of Single Tryptophan Mutants of Chicken Skeletal Troponin C: Evidence for Interdomain Interaction
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology, Mayo Foundation, 200 First Street SW, Rochester, Minnesota 55905, and Department of Molecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, Florida 33101
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi982048j
Reference73 articles.
1. Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution.
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2. Allosteric Transmission along a Loosely Structured Backbone Allows a Cardiac Troponin C Mutant to Function with Only One Ca2+ Ion;Journal of Biological Chemistry;2017-02
3. Cardiac Troponin and Tropomyosin: Structural and Cellular Perspectives to Unveil the Hypertrophic Cardiomyopathy Phenotype;Frontiers in Physiology;2016-09-23
4. Insights into the Intramolecular Coupling between the N- and C-Domains of Troponin C Derived from High-Pressure, Fluorescence, Nuclear Magnetic Resonance, and Small-Angle X-ray Scattering Studies;Biochemistry;2012-12-19
5. The biochemical effect of Ser166 phosphorylation on Euplotes octocarinatus centrin;JBIC Journal of Biological Inorganic Chemistry;2012-11-23
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