Structural propensities in the heme binding region of apocytochrome b5. I. Free peptides
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
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1. Utility of heme analogues to intentionally modify heme–globin interactions in myoglobin;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2016-05
2. Accommodating a Nonconservative Internal Mutation by Water-Mediated Hydrogen Bonding between β-Sheet Strands: A Comparison of Human and Rat Type B (Mitochondrial) Cytochrome b5;Biochemistry;2011-05-26
3. Folding behaviors of apocytochrome b5 and its mutants: Insights from high temperature molecular dynamics simulations;Journal of Molecular Structure: THEOCHEM;2009-09
4. Preparation of a biologically active apo-cytochrome b5 via heterologous expression in Escherichia coli;Protein Expression and Purification;2009-08
5. Structural propensities in the heme binding region of apocytochrome b5. II. Heme conjugates;Biopolymers;2008
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