NDLI: Tryptophan dynamics in the exploration of micro-conformational changes of refolded ß-lactoglobulin after thermal exposure: a steady state and time-resolved fluorescence approach.

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Tryptophan dynamics in the exploration of micro-conformational changes of refolded ß-lactoglobulin after thermal exposure: a steady state and time-resolved fluorescence approach.

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Tryptophan dynamics in the exploration of micro-conformational changes of refolded ß-lactoglobulin after thermal exposure: a steady state and time-resolved fluorescence approach.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Halder, Umesh C. Chakraborty, Jishnu Das, Niloy Bose, Sayantan
Description	Country affiliation: India Author Affiliation: Halder UC ( Organic Chemistry Section, Department of Chemistry, Jadavpur University, 188, Raja S.C. Mullik Road, Jadavpur, Kolkata 700 032, West Bengal, India. uhalder2002@yahoo.com)
Abstract	Refolding intermediates of proteins, including molten globules, are likely to undergo dynamic conformational transitions. In this work, thermal unfolding and refolding of bovine ß-lactoglobulin (ß-lg) have been revisited to encounter such intermediate states. Lower thermal range (< 80°C) was selected to avoid irreversible aggregate formation. The gross kinetic refolding as monitored with the fluorophore, Trp19, was likely to be reversible but alteration in time resolved fluorescence parameters ruled out the possibility of micro-structural reversibility for the refolded partner. Time resolved fluorescence showed that the refolded protein still lacks some intact native conformation. Far-UV CD signals lack the signature of any secondary structural distortion in global structural context whereas near-UV CD signals were strongly indicative of perturbation in micro-structure surrounding the aromatic moieties which hardly revives after cooling. Steady state anisotropy results showed successfully the break-down of dimer to monomer form of ß-lg within 50°C temperature range and augmentation in anisotropy up on further thermal stress reflected the reorganization of tryptophan residues into more restricted and rigid micro-environment as well as irreversible disulfide-linked dimer formation. Reliability of conformational reversibility in the thermal unfolding-refolding is still enigmatic on micro and global structural perspectives. Intermediate state prior to the completion of refolding of thermally exposed ß-lg was identified through fluorescence studies.
File Format	HTM / HTML
ISSN	10111344
Volume Number	109
e-ISSN	18732682
Journal	Journal of Photochemistry and Photobiology B: Biology
Language	English
Publisher	Elsevier
Publisher Date	2012-04-02
Publisher Place	Switzerland
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biology Hot Temperature Lactoglobulins Chemistry Protein Refolding Spectrometry, Fluorescence Methods Tryptophan Animals Cattle Fluorescence Polarization Models, Molecular Protein Conformation Protein Unfolding Time Factors Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Radiology, Nuclear Medicine and Imaging Biophysics Radiological and Ultrasound Technology Radiation

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