NMR Analysis Shows That a b-Type Variant of Hydrogenobacter thermophilus Cytochrome c552 Retains Its Native Structure
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. Cytochromes c: Evolutionary, Structural, and Physicochemical Aspects;Pettigrew,1991
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1. Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2016-05
2. Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c 552 and its b-type variant;Journal of Biomolecular NMR;2015-05-08
3. Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers;Chemical Reviews;2014-04-23
4. Influence of Heme Post-Translational Modification and Distal Ligation on the Backbone Dynamics of a Monomeric Hemoglobin;Biochemistry;2012-07-09
5. Temperature Dependent Equilibrium Native to Unfolded Protein Dynamics and Properties Observed with IR Absorption and 2D IR Vibrational Echo Experiments;Journal of the American Chemical Society;2011-04-06
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