<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Jagtap, Sharmili</style></author><author><style face="normal" font="default" size="100%">Rao, Mala</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Fluorescence study on interactions of alpha-crystallin with the molten globule state of 1, 4-beta-D-glucan glucanohydrolase from thermomonospora sp induced by guanidine hydrochloride</style></title><secondary-title><style face="normal" font="default" size="100%">Journal of Fluorescence</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">ANS</style></keyword><keyword><style  face="normal" font="default" size="100%">Cellulase</style></keyword><keyword><style  face="normal" font="default" size="100%">Guanidine hydrochloride</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein folding</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">6</style></number><publisher><style face="normal" font="default" size="100%">SPRINGER/PLENUM PUBLISHERS</style></publisher><pub-location><style face="normal" font="default" size="100%">233 SPRING ST, NEW YORK, NY 10013 USA</style></pub-location><volume><style face="normal" font="default" size="100%">19</style></volume><pages><style face="normal" font="default" size="100%">967-973</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;In this paper, the interaction between alpha- crystallin and molten globule structure of 1,4-beta-D-Glucan Glucohydrolase (TSC) from an alkalothermophilic Thermomonospora sp. was investigated mainly by fluorescence quenching spectra, circular dichroism and three dimensional fluorescence spectra under simulative physiological conditions. Denaturation studies using GdnCl indicated that TSC folds through a partially folded state that resembles molten globule at 1.8 M GdnCl. The chaperone activity of alpha- crystallin was employed to study refolding of TSC. Here we studied the refolding of GdnCl denatured TSC from its molten globule state (TSC-m complex) in the presence and absence of alpha-crystallin to elucidate the molecular mechanism of chaperone-mediated in vitro folding. Our results, based on intrinsic tryptophan fluorescence and ANS binding studies, suggest that alpha-crystallin formed a complex with a putative intermediate molten globule - like intermediate in the refolding pathway of TSC. Reconstitution of the active TSC was observed on cooling the alpha-crystallin aEuro cent TSC -m complex to 4A degrees C. Addition of alpha-crystallin to the molten globule - like intermediate of TSC (TSC-m complex) complex initiated the refolding of TSC with 69 % recovery of the biological activity of the enzyme.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">6</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">1.966</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Kumar, Avinash</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Multistate unfolding of alpha-mannosidase from Canavalia ensiformis (Jack Bean): evidence for the thermostable molten globule</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemical and Biophysical Research Communications</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">alpha-Mannosidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Circular dichroism</style></keyword><keyword><style  face="normal" font="default" size="100%">fluorescence</style></keyword><keyword><style  face="normal" font="default" size="100%">Guanidine hydrochloride</style></keyword><keyword><style  face="normal" font="default" size="100%">Molten globule</style></keyword><keyword><style  face="normal" font="default" size="100%">Thermostability</style></keyword><keyword><style  face="normal" font="default" size="100%">Unfolding</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3-4</style></number><publisher><style face="normal" font="default" size="100%">ACADEMIC PRESS INC ELSEVIER SCIENCE</style></publisher><pub-location><style face="normal" font="default" size="100%">525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA</style></pub-location><volume><style face="normal" font="default" size="100%">403</style></volume><pages><style face="normal" font="default" size="100%">391-397</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;The relevance of partially ordered states of proteins (such as the molten-globule state) in cellular processes is beginning to be understood. We examined the conformational transitions in a multimeric and high molecular weight class II alpha-mannosidase from Canavalia ensiformis (Jack Bean) (Jb alpha-man) utilizing intrinsic fluorescence, solute quenching, hydrophobic dye binding, size exclusion chromatography and circular dichroism (CD) spectroscopy for the protein in presence of Guanidine hydrochloride (GdnHCl). The decomposition analysis of the protein spectra obtained during unfolding showed progressive appearance of class S, I, II and III trp. The parameter A and spectral center of mass showed multi state unfolding of the protein and phase diagram analysis revealed formation of an intermediate of Jb alpha-man in the vicinity of 1 M GdnHCl. The intermediate exhibited compact secondary and distorted tertiary structure with exposed hydrophobic amino acids on the surface, indicating the molten-globule nature. The dissociation, partial unfolding and aggregation of Jb alpha-man occurred simultaneously during chemical denaturation. The molten-globule possessed slightly higher hydrodynamic radius, perturbance in the structure up to 60 degrees C and stability of the structure up to 80 degrees C unlike the native Jack Bean alpha-mannosidase. The modes of chemical and thermal denaturation of the native protein were different. The solute quenching parameters confirmed the altered confirmation of the intermediate. Taken together, our results constitute one of the early reports of formation of GdnHCl induced molten globule in a class II alpha-mannosidase. (C) 2010 Elsevier Inc. All rights reserved.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3-4</style></issue><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">2.595</style></custom4></record></records></xml>