@article { ISI:000245984200011,
	title = {Bile salt hydrolase, the member of Ntn-hydrolase family: differential modes of structural and functional transitions during denaturation},
	journal = {IUBMB Life},
	volume = {59},
	number = {2},
	year = {2007},
	month = {FEB},
	pages = {118-125},
	publisher = {TAYLOR \& FRANCIS INC},
	type = {Article},
	address = {325 CHESTNUT ST, SUITE 800, PHILADELPHIA, PA 19106 USA},
	abstract = {<p>Conformational transitions and functional stability of the bile salt hydrolase (BSH; cholylglycine EC: 3.5.1.24) from Bifidobacterium longum (BlBSH) cloned and expressed in E. coli were studied under thermal, chemical and pH-mediated denaturation conditions using fluorescence and CD spectroscopy. Thermal and Gdn-HCl-mediated denaturation of BlBSH is a multistep process of inactivation and unfolding. The inactivation and unfolding of the enzyme was found to be irreversible. Enzyme activity seems sensitive to even minor conformational changes at the active site. Thermal denaturation as such did not result in any insoluble protein aggregates. However, on treating with 0.25-1 M Gdn-HCl the enzyme showed increasing aggregation at temperatures of 40-55 degrees C indicating more complex structural changes taking place in the presence of chemical denaturants. The enzyme secondary structure was still intact at acidic pH (pH 1-3). The perturbation in the tertiary structure at the acidic pH was detected through freshly formed solvent exposed hydrophobic patches on the enzyme. These changes could be due to the formation of an acid-induced molten globule-like state.</p>},
	keywords = {Aggregation, Bile salt hydrolase, molten-globule, Unfolding},
	issn = {1521-6543},
	doi = {10.1080/15216540701245014},
	author = {Kumar, R. Suresh and Suresh, C. G. and Brannigan, James A. and Dodson, Guy G. and Gaikwad, Sushama M.}
}
@article { ISI:000291061500032,
	title = {Conformational transitions in ariesaema curvatum lectin: characterization of an acid induced active molten globule},
	journal = {Journal of Fluorescence},
	volume = {21},
	number = {2},
	year = {2011},
	month = {MAR},
	pages = {753-763},
	publisher = {SPRINGER/PLENUM PUBLISHERS},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>Biophysical characterization of a lectin from Ariesaema curvatum (ACL) was carried out using steady state as well as time resolved fluorescence and CD spectroscopy under various denaturing conditions. An intermediate with altered tryptophan microenvironment was detected in the phase diagram, which exibited pronounced secondary structure and hemagglutinating activity in presence of 0.25 M Gdn-HCl. An acid induced molten- globule like structure possessing activity and higher thermostability was detected. Transition to the molten globule state was reversible in nature. The lectin retained hemagglutinating activity even after incubation at 95 A degrees C. Both chemical and thermal unfolding of the lectin were found to consist of multistate processes. Fluorescence quenching of ACL was strong with acrylamide and KI. The single tryptophan was found to be surrounded by high density of the positively charged amino acid residues as shown by a ten fold higher K(sv) for KI compared to that for CsCl. The average lifetime of tryptophan fluorescence increased from 1.24 ns in the native state to 1.72 ns in the denatured state.</p>},
	keywords = {Araceae, Fluorescence lifetime, Hemagglutinin, Molten globule, Secondary structure, Thermostability, Unfolding},
	issn = {1053-0509},
	doi = {10.1007/s10895-010-0766-2},
	author = {Sharma, Urvashi and Gaikwad, Sushama M. and Suresh, C. G. and Dhuna, Vikram and Singh, Jatinder and Kamboj, Sukhdev Singh}
}
