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Arginine inhibits aggregation of alpha-lactalbumin but also decreases its stability: Calorimetric, spectroscopic, and molecular dynamics studies

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Title Arginine inhibits aggregation of alpha-lactalbumin but also decreases its stability: Calorimetric, spectroscopic, and molecular dynamics studies
 
Creator KUMAR, N
KISHORE, N
 
Subject Protein stabilization
Isothermal titration calorimetry
Differential scanning calorimetry
Radial distribution function
Hydrogen bond dynamics
EMPIRICAL FORCE-FIELD
AMINO-ACID SEQUENCE
PROTEIN AGGREGATION
ESCHERICHIA-COLI
MIXED-SOLVENTS
NUCLEIC-ACIDS
THIOFLAVIN-T
MECHANISM
LYSOZYME
UREA
 
Description Arginine (Arg) has long been used to inhibit aggregation of proteins. Despite its frequent use in inhibition of aggregation, the exact mechanism of aggregation and the effect of Arg on the conformation and stability of proteins are still not well understood. In the present study, spectroscopic, calorimetric, and molecular dynamics methods have been used to understand the mechanism of inhibition of aggregation of alpha-lactalbumin (alpha-LA) by Arg along with its effect on stability of the protein. It is observed that although Arg inhibits aggregation of alpha-LA, it also decreases stability of the protein. The results suggest that strong favorable interactions between alpha-LA and guanidinium group of Arg decrease the stability of the protein. The results also suggest that the guanidinium group preferentially interacts with Gln, Asn and negatively charged residues through hydrogen bonding and electrostatic interactions. (C) 2014 Elsevier Ltd. All rights reserved.
 
Publisher ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
 
Date 2014-12-28T11:14:24Z
2014-12-28T11:14:24Z
2014
 
Type Article
 
Identifier JOURNAL OF CHEMICAL THERMODYNAMICS, 78159-166
0021-9614
1096-3626
http://dx.doi.org/10.1016/j.jct.2014.06.024
http://dspace.library.iitb.ac.in/jspui/handle/100/16331
 
Language English