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  • About
  • The Global ETD Search service is a free service for researchers to find electronic theses and dissertations. This service is provided by the Networked Digital Library of Theses and Dissertations.
    Our metadata is collected from universities around the world. If you manage a university/consortium/country archive and want to be added, details can be found on the NDLTD website.

Study of the surface structures and patterns of the hydrophobic-polar model of protein /

Pang, Tin Yau. January 2007 (has links)
Thesis (M.Phil.)--Hong Kong University of Science and Technology, 2007. / Includes bibliographical references (leaves 77-78). Also available in electronic version.

Improvements of protein function annotations using stuctures /

Cheng, Gong, January 2008 (has links)
Thesis (Ph. D.)--University of Washington, 2008. / Vita. Includes bibliographical references (p. 54-66).

Ionic cross-linking reagents and tandem mass spectrometry for mapping structures of proteins and protein complexes

Lu, Yali. January 2008 (has links)
Thesis (M.S.)--Michigan State University. Dept. of Chemistry, 2008. / Title from PDF t.p. (Proquest, viewed on Aug. 11, 2009) Includes bibliographical references (p. 93-99).

Towards a comprehensive human protein-protein interaction network

Ramani, Arun Kumar. January 2005 (has links) (PDF)
Thesis (Ph. D.)--University of Texas at Austin, 2005. / Vita. Includes bibliographical references.

Protein retention and transport in hydrophobic interaction chromatography

To, Chi Shung Brian. January 2006 (has links)
Thesis (Ph.D.)--University of Delaware, 2006. / Principal faculty advisor: Abraham M. Lenhoff, Dept. of Chemical Engineering. Includes bibliographical references.

The targeting mechanism and membrane topology of tail-anchored proteins /

Kim, Peter K. Andrews, D. W. January 1900 (has links)
Thesis (Ph. D.)--McMaster University, 2003. / Adviser: D. W. Andrews. Includes bibliographical references. Also available via World Wide Web.

Self assembly studies of native and recombinant fibrous proteins /

Wilson, Donna L. January 1900 (has links)
Thesis (Ph.D.)--Tufts University, 2003. / Adviser: David L. Kaplan. Submitted to the Dept. of Chemistry and Biotechnology. Includes bibliographical references (leaves 203-210). Access restricted to members of the Tufts University community. Also available via the World Wide Web;

The role of the domain interface in the stability, folding and function of CLIC1

Stoychev, Stoyan Hristov 08 September 2008 (has links)
Chloride intracellular channel protein 1 (CLIC1) is a dual-state protein existing in both soluble monomeric conformation as well as integral-membrane form. The role of the domain interface in the conversion between these species was investigated. Bioinformatics-based analysis was undertaken to compare and contrast the domain interfaces of dimeric GSTs with their monomeric homologues CLIC1 and CLIC4. The mutants CLIC1-M32A and CLIC1-E81M were used as experimental case studies on the role of domain-domain interactions in the stability and folding of CLIC family proteins. A consensus interface was revealed with the prominent interaction being a conserved inter-domain lock-and-key type motif previously studied in class Alpha GSTs (Wallace et al., 2000). A number of domain-interface interactions were found to be unique to the CLIC family and as such thought to play a role in the conversion of these proteins from their soluble form to an integral membrane form. Overall the domain interfaces of monomeric CLIC1 and CLIC4 did not differ significantly from the domain interfaces of dimeric GSTs. The removal of the unique CLIC family salt-bridges between Arg29 and Glu81 and the cavity forming domain interface mutation Met32Ala did not induce significant changes in the conformational flexibility of the native state. The true role of the Arg29-Glu81 salt-bridges was masked by the introduction of stabilizing hydrophobic contacts. Removal of the inter-domain lock-and-key interaction destabilized CLIC1 significantly with concomitant loss in cooperative folding that resulted in the stabilization of a molten globule-like species. This intermediate state was less stable and less structured than the equilibrium intermediate of wtCLIC1 at pH 5.5. However the bulk of the structures found to unfold during intermediate-species formation was the same in mutant and wild-type proteins. It was concluded that formation of the membrane-competent form of CLIC1 involves re-structuring of the N-terminal thioredoxin domain that takes place after destabilization of the salt bridges connecting h1 and h3 and uncoupling of the inter-domain lock-and-key motif.

Molecular and functional characterization of a novel ring-H2 finger protein, ANAPC11, the anaphase-promoting complex subunit 11. / CUHK electronic theses & dissertations collection

January 2003 (has links)
by Chan Hei. / "July 2003." / Thesis (Ph.D.)--Chinese University of Hong Kong, 2003. / Includes bibliographical references (p. 235-247). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Mode of access: World Wide Web. / Abstracts in English and Chinese.

Protein molecules are small

18 March 2013 (has links)
My theory is that protein molecules are very small.

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