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Heme orientation affects holo-myoglobin folding and unfolding kinetics

Native myoglobin (Mb) consists of two populations which differ in the orientation of the heme by 180° rotation (as verified by nuclear magnetic resonance) but have identical absorption spectra and equilibrium–thermodynamic stability. Here, we report that these two fractions of native oxidized Mb (fr...

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Published in:	FEBS letters 2000-03, Vol.470 (2), p.203-206
Main Authors:	Moczygemba, Charmaine, Guidry, Jesse, Wittung-Stafshede, Pernilla
Format:	Article
Language:	English
Subjects:	Animals Apoproteins - chemistry Apoproteins - metabolism Circular Dichroism Dose-Response Relationship, Drug Fluorescence Guanidine - pharmacology Heme - metabolism Heme protein Horses Kinetics Metmyoglobin - chemistry Metmyoglobin - metabolism Myoglobin Myoglobin - chemistry Myoglobin - metabolism Protein Denaturation - drug effects Protein Folding Protein Renaturation Rotation Stopped-flow mixing Thermodynamics Tryptophan - metabolism Whales
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creator	Moczygemba, Charmaine Guidry, Jesse Wittung-Stafshede, Pernilla
description	Native myoglobin (Mb) consists of two populations which differ in the orientation of the heme by 180° rotation (as verified by nuclear magnetic resonance) but have identical absorption spectra and equilibrium–thermodynamic stability. Here, we report that these two fractions of native oxidized Mb (from horse) both unfold and refold (chemical denaturant, pH 7, 20°C) in two parallel kinetic reactions with rate constants differing 10-fold. In accord, the oxidized heme remains coordinated to unfolded horse Mb in up to 4 M guanidine hydrochloride (pH 7, 20°C).
doi_str_mv	10.1016/S0014-5793(00)01319-3
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subjects	Animals Apoproteins - chemistry Apoproteins - metabolism Circular Dichroism Dose-Response Relationship, Drug Fluorescence Guanidine - pharmacology Heme - metabolism Heme protein Horses Kinetics Metmyoglobin - chemistry Metmyoglobin - metabolism Myoglobin Myoglobin - chemistry Myoglobin - metabolism Protein Denaturation - drug effects Protein Folding Protein Renaturation Rotation Stopped-flow mixing Thermodynamics Tryptophan - metabolism Whales
title	Heme orientation affects holo-myoglobin folding and unfolding kinetics
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