Vacuum-Ultraviolet Circular Dichroism Spectra of Escherichia coli Dihydrofolate Reductase and Its Mutants: Contributions of Phenylalanine and Tyrosine Side Chains and Exciton Coupling of Two Tryptophan Side Chains

Vacuum-ultraviolet (VUV) circular dichroism (CD) spectroscopy has recently been used for secondary structure analysis of proteins; however, the contribution of aromatic side chains to protein VUV CD spectra is unresolved. In this report, VUV CD spectra of 10 Escherichia coli dihydrofolate reductase...

Full description

Bibliographic Details

Published in:	The journal of physical chemistry. B Vol. 119; no. 41; pp. 13002 - 13008
Main Authors:	Ohmae, Eiji, Tanaka, Suguru, Miyashita, Yurina, Katayanagi, Katsuo, Matsuo, Koichi
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 15-10-2015
Subjects:	Circular Dichroism - methods Dichroism Escherichia coli - enzymology Excitation spectra Joining Mutation Phenylalanine Proteins Reductases Spectra Spectrophotometry, Ultraviolet - methods Tetrahydrofolate Dehydrogenase - chemistry Tetrahydrofolate Dehydrogenase - genetics Tryptophan - chemistry Tyrosine
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!