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Showing 1 to 8 of 8 for “"multidomain proteins"”.
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Computational discovery and modelling of tandem domain repeats in proteins
Domains are functional and evolutionary units of proteins that typically fold into stable globular structures. A small subset of natural multidomain proteins contain large arrays of nearly identical domains repeated in tandem, challenging some of our assumptions about protein folding and evolution. …
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Vesicular stomatitis virus induced apoptosis occurs by a mechanism involving the activation of pro-apoptotic Bcl-2 proteins Bak and Bid and the inactivation of anti-apoptotic Bcl-2 proteins Bcl-XL and Mcl-1
… I address the question of what role Bcl-2 family proteins play in apoptosis induced by vesicular stomatitis virus (VSV) with wild-type (wt) M protein (rWT virus). My results demonstrate that of the two major proapoptotic multidomain proteins Bak and Bax, Bak is more important for the induction of …
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Engineering functional recombinant proteins based on antibody domains and fragments of C. botulinum neurotoxin
… and properties of novel recombinant targeted multidomain proteins. Single chain Fv’s consist of a VH region of heavy chain linked by a stretch of synthetic peptide to a VL region of the light chain. Fv is the region for binding to antigens as determined by immunoglobulin Ig hypervariable …
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Gene expression studies of pregastrulation development: the basement membrane is essential for cell differentiation
… and disease. Laminins, a major BM component, are multidomain proteins, consisting of three polypeptide chains (α, β and γ). During pregastrulation development, stem cells convert and epithelial tissues are formed. This process is faithfully mimicked in vitro by embryoid body (EB) cultures. …
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Function and Properties of groE Chaperonins in Bacterial and Mammalian Cells
… most polypeptides <em>in vivo</em>, and protect proteins against aggregation when a cell is under stress. The GroESL proteins of <em>Escherichia coli</em> are the best characterized of the ringed chaperones, or chaperonins. Chaperonins of the eukaryotic cytoplasm interact with a limited number of …
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New experimental and theoretical tools for studying protein systems with elements of structural disorder
<p>Disordered proteins are one class of proteins which do not possess well-folded three-dimensional structures as their native conformations. Many eukaryotic proteins have been found to be fully disordered or contain certain disordered regions. Disordered proteins usually display several …
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Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli
… site. Finally it is found as a member of many multidomain proteins. Although some members of this family of proteins show sulfurtransferase activity in vitro, their specific physiological functions remain largely undefined. Fusion of a rhodanese domain to different protein domains of known or …
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STRUCTURE-FUNCTION STUDIES OF NOVEL MEDICALLY RELEVANT FLAVOENZYMES
Flavoproteins are involved in a wide range of biological processes, with a variety of catalytic reactions performed, which range from typical redox catalyses such as the dehydrogenation of an amino acid, or activation of dioxygen, to photochemistry; from DNA damage repair to light emission. …