Time‐resolved circular dichroism in carbonmonoxy‐myoglobin: The central role of the proximal histidine | Zendy

Dartigalongue Thibault | Zendy; Hache François | Zendy

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Time‐resolved circular dichroism in carbonmonoxy‐myoglobin: The central role of the proximal histidine

Author(s) -

Dartigalongue Thibault,

Hache François

Publication year - 2006

Publication title -

chirality

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.43

H-Index - 77

eISSN - 1520-636X

pISSN - 0899-0042

DOI - 10.1002/chir.20254

Subject(s) - myoglobin , chemistry , histidine , circular dichroism , crystallography , stereochemistry , amino acid , biochemistry

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. Chirality, 2006. © 2006 Wiley‐Liss, Inc.

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