Global ETD Search

81	Investigations into the protein disulphide isomerase-related proteins of Saccharomyces cerevisiae Byrne, Lee J. January 2000 (has links) No description available. 572 Enzymes; PDI; Protein folding
82	Folding and stability studies on papain and the effect of recombinant papain pro fragment Briggs, Geoffrey Shaw January 1994 (has links) No description available. 572 Protein engineering; Protein folding
83	Lysozyme-small molecule interactions Wadoos, Abdul January 1998 (has links) No description available. 572 Benzyl penicillin; Protein folding
84	Folding and assembly studies on the components of mammalian PDC and OGDC McCartney, Richard Graham January 1998 (has links) No description available. 572 Protein biochemistry; Protein folding
85	Characterisation of the endoplasmic reticulum stress proteins GRP78 and GRP94 and their interaction with a recombinant antibody Pearce, Alison January 2000 (has links) No description available. 572 Protein folding; Cell lines
86	Characterisation of the eukaryotic Chaperonin CCT Liou, Anthony Kian-Fong January 1996 (has links) No description available. 572 Eukaryotes; Folding; Tubulins; Actins
87	Peptide models for protein beta-sheets Griffiths-Jones, Samuel R. January 2001 (has links) No description available. 547 Structure; Folding; Misfolding; Disease
88	Engineering Proteins via Peptide Backbone Mutagenesis: The Effects of Thioamide Linkages on the Folding and Stability of Short Peptides Demick, Kristen Ann January 2009 (has links) Thesis advisor: Jianmin Gao / The development of proteins/peptides as therapeutic agents has emerged as a promising area for drug design. Due to increased antibiotic resistance, search for novel antibiotics has become a primary area of interest within the pharmaceutical industry. Antimicrobial peptides have been a significantly desirable model due to their innate cytolytic effects and favorable interaction with the membranes of bacterial cells within the host. Thioxylated analogues of biologically active peptides have shown increased enzymatic stability and increased selectivity and potency. Thioamide linkages have thus been installed in a variety of short peptides, replacing the backbone amide linkage, in order to study the effects on peptide conformation and stability. Several bioanalytical tools were used in the analysis including circular dichroism spectroscopy, NMR, size-exclusion high performance liquid chromatography, and fluorescence. The mutation was well-accommodated within several systems, including Trpzip 4 and gramicidin A, and proved to have comparable, and in several cases, enhanced stability in comparison to the wild-type peptides. / Thesis (MS) — Boston College, 2009. / Submitted to: Boston College. Graduate School of Arts and Sciences. / Discipline: Chemistry. Backbone Folding Peptide Protein Thioamide
89	Biophysical studies of folding and misfolding in tandem repeat proteins Kemplen, Katherine Rosemary January 2015 (has links) No description available. 540 Protein folding ; Physical biochemistry
90	Biological sequence analyses theory, algorithms, and applications / Ma, Fangrui. January 2009 (has links) Thesis (Ph.D.)--University of Nebraska-Lincoln, 2009. / Title from title screen (site viewed October 13, 2009). PDF text: xv, 233 p. : ill. ; 4 Mb. UMI publication number: AAT 3360173. Includes bibliographical references. Also available in microfilm and microfiche formats.

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