Browsing Electronic Theses, Dissertations, and Records of Study (2002– ) by Author "Pace, C. Nick"
Now showing items 1-12 of 12
-
Schmittschmitt, Jason Peter (Texas A&M University, 2004-09-30)The HPr proteins were characterized as folding by a two-state folding mechanism. Here, we present a comparison of the equilibrium and kinetic folding for the HPr protein from Bacillus subtilis, E coli and a key variant ...
-
Syed Ali, Abbas Razvi (Texas A&M University, 2006-04-12)A thermodynamic study of five homologous HPr proteins derived from organisms inhabiting diverse environments has been undertaken. The aim of this study was to further our understanding of protein stabilization in extremes ...
-
Schell, David Andrew (Texas A&M University, 2005-02-17)Properly folded proteins are necessary for all living organisms. Incorrectly folded proteins can lead to a variety of diseases such as Alzheimers Disease or Bovine Spongiform Encephalitis (Mad Cow Disease). Understanding ...
-
Wei, Yun (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 ...
-
Thurlkill, Richard Lee (Texas A&M University, 2007-04-25)A goal of the modern protein chemist is the design of novel proteins with specific activities or functions. One hurdle to overcome is the ability to accurately predict the pKas of ionizable groups upon their burial in the ...
-
Wahlman, Judit (2009-05-15)Secretory proteins that are unable to assemble into native proteins in the endoplasmic reticulum (ER) are transported back into the cytosol for degradation. Many cytosolic and ER resident proteins have been identified so ...
-
Trefethen, Jared M. (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 ...
-
Miles, Jr., George Emmett (Texas A&M University, 2006-08-16)Staphylococcal leukocidin pores are formed by the obligatory interaction of two distinct polypeptides, one of class F and one of class S, making them unique in the family of β-barrel pore-forming toxins (β-PFTs). ...
-
Alston, Roy Willis (Texas A&M University, 2004-09-30)To understand protein stability and the mechanism of protein folding, it is essential that we gain a better understanding of the ensemble of conformations that make up the denatured state of a protein. The primary goal ...
-
Rodriguez Rodriguez, Mauricio (Texas A&M University, 2006-10-30)This manuscript presents a thorough investigation and description of metabolic control dynamics in vivo and in silico using as a model de novo pyrimidine biosynthesis. Metabolic networks have been studied intensely for ...
-
Zhang, Li (Texas A&M University, 2008-10-10)Chemokines (chemotactic cytokines) comprise a large family of proteins that recruit and activate leukocytes, giving chemokines a major role in both immune response and inflammation-related diseases. Viral CC chemokine ...
-
Carson, Kenneth Harris (2009-06-02)Many proteins can easily attain a non-native fold and be of no use or even a detriment to the host. The host cell has a myriad of molecules dedicated to assisting nascent and existing proteins in folding properly and ...