Thumbnail
Access Restriction
Open

Author Morisaku, Toshinori ♦ Arai, Sho ♦ Yui, Hiroharu
Source J-STAGE
Content type Text
Publisher The Japan Society for Analytical Chemistry
Language English
Subject Keyword α-Helix ♦ random-coil ♦ conformational change ♦ hydration ♦ vibrational circular dichroism activity
Abstract Conformational changes of hydrated proteins induced by gradual dehydration were monitored by vibrational circular dichroism (VCD) spectroscopy. In myoglobin and casein, representative α-helix-rich and random-coil proteins, respectively, an increase in left-handed optical activity in the amide I band was detected at the initial stage of dehydration, followed by an increase in opposite right-handed activity in both the amide I and II bands with further dehydration. Because the second step was observed with an increase in the turbidity of the proteins, it can be attributed to their aggregation. In contrast, because the increase in left-handed optical activity is induced by the conformational change of the proteins and is followed by the aggregation, it may derive from the increase in the regularity of the local structure in individual myoglobin or casein that triggers the aggregation.
ISSN 09106340
Learning Resource Type Article
Publisher Date 2014-10-10
e-ISSN 13482246
Journal Analytical Sciences(analsci)
Volume Number 30
Issue Number 10
Page Count 9
Starting Page 961
Ending Page 969


Open content in new tab

   Open content in new tab