Browsing by Subject "protein stability"
Now showing items 1-7 of 7
-
Clostridioides difficile (C. difficile), the microbe responsible for Clostridioides difficile infection (CDI), is a common nosocomial infection that exerts its pathogenicity primarily by two toxins, TcdA and TcdB. Designed ...
-
(2017-07-31)In Drosophila, time-keeping is based on a ~24h transcription feedback loop, in which CLOCK-CYCLE (CLK-CYC) heterodimers activate transcription of genes encoding the feedback repressors PERIOD (PER) and TIMELESS (TIM). ...
-
(2014-11-07)The aim of this study was to investigate the stability contribution of buried ionizable amino acids in proteins. To study the stability contribution of a naturally occurring buried aspartic acid, two stabilized forms of ...
-
(2010-07-14)Proteins need fold to perform their biological function. Thus, understanding how proteins fold could be the key to understanding life. In the first study, the stability and structure of several !-hairpin peptide variants ...
-
(Texas A&M University, 2005-02-17)The primary objective was to study the kinetics of folding of RNase Sa. Wild-type RNase Sa does not contain tryptophan. A tryptophan was substituted at residue 81 (WT*) to allow fluorescence spectroscopy to be used to ...
-
(1990)To study the contribution of disulfide bonds to protein stablity, a derivative of ribonuclease T1 (RNase T1) with both cystine residues reduced and methylated has been prepared using an improved procedure adapted from that ...
-
(Texas A&M University, 2007-09-17)It is critical to consider the balance between the catalytic capabilities of an enzyme and the inherent structural stability of the protein when developing enzymes for specific applications. Rational site directed mutagenesis ...