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dc.contributor.advisorHartson, Steve D.
dc.contributor.authorKalyanaraman, Palgunan
dc.date.accessioned2014-04-15T20:25:34Z
dc.date.available2014-04-15T20:25:34Z
dc.date.issued2006-12-01
dc.identifier.urihttps://hdl.handle.net/11244/8921
dc.description.abstractNewly synthesized proteins must fold to unique three dimensional structures to become functionally active. The native fold of protein is encoded in its amino acid sequence. One of the big challenges of modern science is to uncover the mechanism of protein folding. How the protein folds to a three dimensional structure is still unknown. Anfinsen et al suggested that primary amino acid sequence of proteins has all the information to fold into a native conformation. However, the key to proper folding of proteins lie in the ability of hydrophobic amino acid side.
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dc.languageen_US
dc.publisherOklahoma State University
dc.rightsCopyright is held by the author who has granted the Oklahoma State University Library the non-exclusive right to share this material in its institutional repository. Contact Digital Library Services at lib-dls@okstate.edu or 405-744-9161 for the permission policy on the use, reproduction or distribution of this material.
dc.titleHsp90: Common Target for Diverse Antibiotics
dc.typetext
dc.contributor.committeeMemberMatts, Robert L.
dc.contributor.committeeMemberEssenberg, Richard C.
osu.filenameKalyanaraman_okstate_0664M_1865.pdf
osu.collegeAgricultural Sciences and Natural Resources
osu.accesstypeOpen Access
dc.description.departmentDepartment of Biochemistry and Molecular Biology
dc.type.genreThesis


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