Translator Disclaimer
1 July 2003 Rapid Communication Protein Matrix Elasticity Determined by Fluorescence Anisotropy of Its Tryptophan Residues
Author Affiliations +
Abstract

Rotational motions of Trp residues embedded within human hemoglobin matrix have been measured by using their steady-state fluorescence anisotropy. The mean square angular displacement θ2 of Trp residues, depending on the temperature, can be expressed by

where W is the thermal energy acting on the Trp residues and C the resilient torque constant of the protein matrix. To study the external medium influencing the protein dynamics, comparative experiments were made with protein in aqueous buffer and in the presence of 32% glycerol. The data show that between 5°C and 25°C, external medium acts on the protein matrix elasticity.

Christian Zentz, Jean-Marie Glandières, Sadok El Moshni, and Bernard Alpert "Rapid Communication Protein Matrix Elasticity Determined by Fluorescence Anisotropy of Its Tryptophan Residues," Photochemistry and Photobiology 78(1), 98-102, (1 July 2003). https://doi.org/10.1562/0031-8655(2003)078<0098:RCPMED>2.0.CO;2
Received: 28 April 2003; Accepted: 1 May 2003; Published: 1 July 2003
JOURNAL ARTICLE
5 PAGES

This article is only available to subscribers.
It is not available for individual sale.
+ SAVE TO MY LIBRARY

SHARE
ARTICLE IMPACT
RIGHTS & PERMISSIONS
Get copyright permission
Back to Top