Solvent‐induced Structural Distortions of Horse Metmyoglobin

Structural and dynamic constraints produced by the surrounding solvent on the aquometmyoglobin molecule were investigated by means of circular dichroism and Fourier‐transform infrared spectroscopies, tritium/hydrogen exchange kinetics and small‐angle neutron‐scattering experiments. Formamide and eth...

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Veröffentlicht in:European journal of biochemistry 1995-01, Vol.227 (1‐2), p.241-248
Hauptverfasser: Glandières, Jean‐Marie, Calmettes, Patrick, Martel, Peter, Zentz, Christian, Massat, Alain, Ramstein, Jean, Alpert, Bernard
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container_end_page 248
container_issue 1‐2
container_start_page 241
container_title European journal of biochemistry
container_volume 227
creator Glandières, Jean‐Marie
Calmettes, Patrick
Martel, Peter
Zentz, Christian
Massat, Alain
Ramstein, Jean
Alpert, Bernard
description Structural and dynamic constraints produced by the surrounding solvent on the aquometmyoglobin molecule were investigated by means of circular dichroism and Fourier‐transform infrared spectroscopies, tritium/hydrogen exchange kinetics and small‐angle neutron‐scattering experiments. Formamide and ethanol were chosen as cosolvents because they are known to increase and decrease protein activity, respectively. The CD measurements in the Soret region show that no changes occur in the heme molecular structure nor in the protein near the heme. The results of proton‐exchange kinetics experiments indicate that the conformational dynamics of aquometmyoglobin is only marginally affected by the cosolvents. However, the small‐angle neutron‐scattering spectra strongly suggest that these cosolvents induce some distortions of the tertiary conformation. According to the ultraviolet CD and Fourier‐transform infrared data, the alteration of the tertiary conformation results from changes in both the number of intrachain hydrogen bonds and the structures of β turns of type I' for formamide and of type II for either of the two cosolvents. The use of several techniques allows the present approach to demonstrates that the myoglobin structure is extremely sensitive to its environmental conditions.
doi_str_mv 10.1111/j.1432-1033.1995.tb20381.x
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subjects Animals
Circular Dichroism
conformation change
Fourier‐transform infrared spectroscopy
Hemeproteins - chemistry
Horses
Kinetics
Metmyoglobin - chemistry
mixed solvents
Myoglobin
neutron scattering
Protein Structure, Secondary
Protein Structure, Tertiary
Protons
Solvents
Spectroscopy, Fourier Transform Infrared
title Solvent‐induced Structural Distortions of Horse Metmyoglobin
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