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A denaturation-induced proton-uptake study of horse ferricytochrome c.
Biochem J. 1989 Mar 1;258(2):595-8. doi: 10.1042/bj2580595.
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Determination of the pK for the acid-induced denaturation of ferrocytochrome c.
Biochemistry. 2004 Mar 30;43(12):3564-9. doi: 10.1021/bi036011x.
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Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c.
Biophys J. 1990 Jan;57(1):15-22. doi: 10.1016/S0006-3495(90)82502-9.
7
Denaturant dependence of equilibrium unfolding intermediates and denatured state structure of horse ferricytochrome c.
J Biol Inorg Chem. 2002 Sep;7(7-8):909-16. doi: 10.1007/s00775-002-0381-z. Epub 2002 Jul 5.
10
Proton magnetic resonance studies of horse cytochrome c.
Biochemistry. 1973 Aug 14;12(17):3170-86. doi: 10.1021/bi00741a006.

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Chemoselective Caging of Carboxyl Groups for On-Demand Protein Activation with Small Molecules.
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A Heme Propionate Staples the Structure of Cytochrome for Methionine Ligation to the Heme Iron.
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Naturally Occurring A51V Variant of Human Cytochrome Destabilizes the Native State and Enhances Peroxidase Activity.
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The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c.
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Histidine-Lysine Axial Ligand Switching in a Hemoglobin: A Role for Heme Propionates.
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Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c.
Biochemistry. 2017 Jun 13;56(23):2950-2966. doi: 10.1021/acs.biochem.6b01187. Epub 2017 May 31.
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Resolving the individual components of a pH-induced conformational change.
Biophys J. 2001 Oct;81(4):2331-8. doi: 10.1016/S0006-3495(01)75879-1.

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Control of redox properties of cytochrome c by special electrostatic interactions.
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Structure of rice ferricytochrome c at 2.0 A resolution.
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Structural role of the tyrosine residues of cytochrome c.
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Nuclear-magnetic-resonance studies of ferrocytochrome c. pH and temperature dependence.
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Some aspects of pH and temperature dependence of the NMR spectra of cytochrome C.
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The charge relay system in chymotrypsin and chymotrypsinogen.
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