Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations
authors Reddy, PM; Taha, M; Sharma, YVRK; Venkatesu, P; Lee, MJ
nationality International
journal RSC ADVANCES
keywords TRIMETHYLAMINE-N-OXIDE; UREA-INDUCED DENATURATION; ALPHA-CHYMOTRYPSIN; TRYPTOPHAN FLUORESCENCE; GUANIDINE-HYDROCHLORIDE; PROTEIN STABILITY; GLYCINE BETAINE; PREFERENTIAL INTERACTIONS; CIRCULAR-DICHROISM; OSMOLYTES
abstract Here, circular dichroism (CD) spectroscopy, fluorescence spectroscopy, UV-Vis spectroscopy, SDS-PAGE, substrate SDS-PAGE, and molecular dynamics (MD) simulations techniques have been employed to understand the structural behavioral changes of trypsin (MW: 19.72 kDa, source: digestive system of adult Indian major carp, Catla C. catla) in the presence of various chemical environments. The stability of the trypsin can be increased by stabilizers, including trimethylamine N-oxide (TMAO), proline, and betaine, without affecting its native structure. Trypsin has shown unusual high thermal stability in the presence of betaine. Further, these experimental results were confirmed by means of MD simulations. The present results explicitly elucidated that the behavior of a co-solvent may vary depending upon the type of the protein.
publisher ROYAL SOC CHEMISTRY
issn 2046-2069
year published 2015
volume 5
issue 54
beginning page 43023
ending page 43035
digital object identifier (doi) 10.1039/c5ra01302j
web of science category Chemistry, Multidisciplinary
subject category Chemistry
unique article identifier WOS:000354964600005
  ciceco authors
  impact metrics
journal analysis (jcr 2019):
journal impact factor 3.119
5 year journal impact factor 3.098
category normalized journal impact factor percentile 59.04
dimensions (citation analysis):
altmetrics (social interaction):



 


Apoio

1suponsers_list_ciceco.jpg