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

Résultats de recherche: Contribution à un journal › Article › Revue par des pairs

Résumé

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.

langue originale	Anglais
Pages (de - à)	414-417
Nombre de pages	4
journal	Synthetic Metals
Volume	155
Numéro de publication	2
Les DOIs	https://doi.org/10.1016/j.synthmet.2005.09.026
état	Publié - 15 nov. 2005

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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",

year = "2005",

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T1 - Observation of ultrafast conformational changes in carboxy-myoglobin by time-resolved circular dichroism

AU - Dartigalongue, Thibault

AU - Hache, François

PY - 2005/11/15

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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

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