Time-resolved circular dichroism in carbonmonoxy-myoglobin: the central role of the proximal histidine.

Abstract:

:A calculation of the circular dichroism (CD) spectra of carbonmonoxy- and deoxy-myoglobin is carried out in relation to a time-resolved CD experiment. This calculation allows us to assign a dominant role to the proximal histidine in the definition of the electronic normal modes and to interpret the transient CD structure observed in a strain of the proximal histidine. This strain builds up in 10 ps and relaxes in 50 ps as the protein evolves towards its deoxy form.

journal_name

Chirality

journal_title

Chirality

authors

Dartigalongue T,Hache F

doi

10.1002/chir.20254

subject

Has Abstract

pub_date

2006-05-05 00:00:00

pages

273-8

issue

4

eissn

0899-0042

issn

1520-636X

journal_volume

18

pub_type

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