Cytochrome c551 as a model system for protein folding
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,Biophysics
Reference53 articles.
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1. Protein Folding Modulates the Swapped Dimerization Mechanism of Methyl-Accepting Chemotaxis Heme Sensors;PLoS ONE;2012-09-28
2. Conferment of Folding Ability to a Naturally Unfolded Apocytochrome c through Introduction of Hydrophobic Amino Acid Residues;Biochemistry;2011-03-04
3. Fast folding kinetics and stabilization of apo-cytochromec;FEBS Letters;2008-02-26
4. Characterization of Non-Native Heme Coordination Structures Emerging upon Guanidine Hydrochloric Acid-Induced Unfolding ofPseudomonas aeruginosaFerricytochromec551;Bulletin of the Chemical Society of Japan;2005-11
5. 1H NMR studies of paramagnetic ferricytochrome c-551 from Pseudomonas aeruginosa at high pH: The role of histidine 16 in the spin transition;Polyhedron;2005-10
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