Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 13 of 13 for “"Folding stability"”.
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Structural constraints for the folding, stability and function of cytochrome C
The relationship between structure, stability and function in yeast (Saccharomyces cerevisiae) cytochrome c was studied through the investigation of mutant proteins. Two isozymes of cyto-chrome c can be isolated from yeast, iso-1 and iso-2-cytochrome c. The structure of iso-l-cyto-chrome c had been …
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Folding, stability and aggregation of the long-lived eye lens protein human gamma D crystallin
… regenerate during life, thus necessitating high stability and solubility. Covalent damage, including glutamine deamidation, of the lens crystallins increases with age and as a result of exposure to environmental insults. Such covalent damage may cause partial-unfolding into aggregation-prone …
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Development and Application of Large-Scale Protein Folding Stability Analysis in Drug Target Identification and Disease Biomarker Discovery
… for the large-scale analysis of protein folding stabilities. The main focus of this dissertation is to develop and apply these large-scale protein folding stability approaches in drug target identification and disease biomarker discovery. One goal of this work is to develop a novel …
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Contributions of aromatic pairs of human Gamma-D-Crystallin to its folding, stability, aggregation, and interaction with human Alpha B-Crystallin
… lens soluble proteins. Long-term solubility and stability against unfolding and aggregation are essential properties of crystallins and crucial to the function of the lens. Aggregation of crystallins in the lens causes light scattering and directly contributes to development of cataract, the …
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Protein folding in crowded environments and living cells
Biomolecular dynamics and stability are predominantly investigated in vitro, and extrapolated to explain function in the living cell. In this thesis, we attempt to bridge this divide by performing studies of protein folding in in vitro crowded environments and in living cells. We begin by …
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Advancing fast relaxation imaging to determine protein stability and folding kinetics on poly(n-isopropyl acrylamide) films
… this assumes that PNIPAM does not perturb the stability of biomolecules. Previous analytical and spectroscopic techniques have not been able to confirm this assumption due to limitations in detection of proteins on surfaces. Additionally, protein absorption above the lower critical solution …
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Molecular and genetic characterization of spinocerebellar ataxia type 5 (SCA5)
… effects of the German SCA5 mutation on protein folding, stability and function. These experiments demonstrate that the leucine to proline substitution causes a temperature sensitive misfolding of the protein, rendering it insoluble and subject to degradation. Additionally, the mutation likely …
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Protein structure determination using evolutionary information
… For protein-coding genes, the task includes folding, stability, and function. The record of the evolutionary process, which in itself is probabilistic, is contained within a multiple sequence alignment. A statistical model that accurately describes these evolutionary constraints for a given …
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Insights Into The Reactivation, Regulation and Essentiality of Oxidative Protein Folding Pathways In Actinobacteria
… disulfide bond formation is important for proper folding, stability and function of exported proteins. The process of disulfide bond formation, termed oxidative protein folding, is catalyzed by thiol-disulfide oxidoreductase enzymes. Oxidative protein folding pathways influence processes essential …
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Covalent Modification that Enhances Protein Properties and Functions and Folds Random Coil into Alpha-Helix
… is to modify proteins covalently to induce folding in random coil sequences, prevent aggregation, surface adsorption and for increasing the thermal stability against aggregation of proteins.</p> <p>The first chapter describes the chemistry for modifying the lysine residues in proteins with …
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Assembly and substrate recognition properties of human CCT subunits of the TRiC chaperonin
… [alpha] (1) - [theta] (8). TRiC is necessary for folding about 10% of newly synthesized proteins and is essential for folding actin and tubulin. Most of the research on TRiC in the last 20 years has focused on yeast and bovine TRiC. However, recently, there has been inquiry into TRiC as a target …
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Toward accurate free energy calculations in biomolecular simulation: advances in Markov model reweighting and expanded ensemble method
… and $³J_H^N$ $H^\alpha$ couplings. The resulting folding landscapes accurately capture the effects of subtle chemical modifications on stability (≤2 kJ/mol changes), aligning with experimental trends and outperforming prior NAMFIS estimates, demonstrating robustness for experiment-guided …
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Isomerization-Locked Alkene Analogues of Xaa–Pro Dipeptides in the Proteins Collagen and Bora
… is the rate-limiting step in collagen folding. However, eliminating isomerization with a trans-locked alkene isostere destabilizes collagen-like peptides. Collagen is stabilized by electronic interactions, namely the n→π* interaction. Halo-alkene isosteres may be used to recapture these …