Observation of ultrafast conformational changes in carboxy-myoglobin by time-resolved circular dichroism

Thibault Dartigalongue; François Hache

doi:10.1016/j.synthmet.2005.09.026

Observation of ultrafast conformational changes in carboxy-myoglobin by time-resolved circular dichroism

Thibault Dartigalongue
, François Hache

Institut Polytechnique de Paris

Research output: Contribution to journal › Article › peer-review

Abstract

A time-resolved circular dichroism experiment is carried out on carboxy-myoglobin. CD is measured with a sub-picosecond time resolution after ligand dissociation. We observe a decrease of the CD signal in a few picoseconds followed by a 100 ps relaxation towards the deoxy-myoglobin values. Thanks to a calculation developed after the polarizability theory, we are able to assign this signal to a global reorganization of the protein conformation.

Original language	English
Pages (from-to)	414-417
Number of pages	4
Journal	Synthetic Metals
Volume	155
Issue number	2
DOIs	https://doi.org/10.1016/j.synthmet.2005.09.026
Publication status	Published - 15 Nov 2005

Keywords

Optical absorption and emission spectroscopy (UV-vis-NIR absorption)
Time-resolved fast spectroscopy

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10.1016/j.synthmet.2005.09.026

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title = "Observation of ultrafast conformational changes in carboxy-myoglobin by time-resolved circular dichroism",

abstract = "A time-resolved circular dichroism experiment is carried out on carboxy-myoglobin. CD is measured with a sub-picosecond time resolution after ligand dissociation. We observe a decrease of the CD signal in a few picoseconds followed by a 100 ps relaxation towards the deoxy-myoglobin values. Thanks to a calculation developed after the polarizability theory, we are able to assign this signal to a global reorganization of the protein conformation.",

keywords = "Optical absorption and emission spectroscopy (UV-vis-NIR absorption), Time-resolved fast spectroscopy",

author = "Thibault Dartigalongue and Fran{\c c}ois Hache",

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AU - Dartigalongue, Thibault

AU - Hache, François

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N2 - A time-resolved circular dichroism experiment is carried out on carboxy-myoglobin. CD is measured with a sub-picosecond time resolution after ligand dissociation. We observe a decrease of the CD signal in a few picoseconds followed by a 100 ps relaxation towards the deoxy-myoglobin values. Thanks to a calculation developed after the polarizability theory, we are able to assign this signal to a global reorganization of the protein conformation.

AB - A time-resolved circular dichroism experiment is carried out on carboxy-myoglobin. CD is measured with a sub-picosecond time resolution after ligand dissociation. We observe a decrease of the CD signal in a few picoseconds followed by a 100 ps relaxation towards the deoxy-myoglobin values. Thanks to a calculation developed after the polarizability theory, we are able to assign this signal to a global reorganization of the protein conformation.

KW - Optical absorption and emission spectroscopy (UV-vis-NIR absorption)

KW - Time-resolved fast spectroscopy

U2 - 10.1016/j.synthmet.2005.09.026

DO - 10.1016/j.synthmet.2005.09.026

M3 - Article

AN - SCOPUS:28544444150

SN - 0379-6779

VL - 155

SP - 414

EP - 417

JO - Synthetic Metals

JF - Synthetic Metals

IS - 2

ER -

Observation of ultrafast conformational changes in carboxy-myoglobin by time-resolved circular dichroism

Abstract

Keywords

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