Biophysical characterization of protein folding and misfolding.

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dc.contributor.advisor Scholtz , J . Martin en_US
dc.contributor.committeeMember LiWang , Andy C . en_US
dc.creator Schmittschmitt , Jason Peter en_US
dc.date.accessioned 2004 -09 -30T01 :40 :52Z
dc.date.accessioned 2014 -02 -18T22 :28 :05Z
dc.date.available 2004 -09 -30T01 :40 :52Z
dc.date.available 2014 -02 -18T22 :28 :05Z
dc.date.created 2003 -12 en_US
dc.date.issued 2004 -09 -30T01 :40 :52Z
dc.identifier.uri http : / /hdl .handle .net /1969 .1 /46
dc.description.abstract The HPr proteins were characterized as folding by a two -state folding mechanism . Here , we present a comparison of the equilibrium and kinetic folding for the HPr protein from Bacillus subtilis , E coli and a key variant from these proteins . For the wild -type protein we find that GHX is greater than GUDC , suggesting that the HPr does not fold by a simple two -state mechanism . This discrepancy is revealed by testing the two -state nature of the folding reaction of HPr with mutation . We show that removing a single charge side chain (Asp 69 ) converts the HPr protein back to a simple two -state mechanism . Ribonuclease Sa and two charge -reversal variants can be converted into amyloidin vitro by the addition of 2 ,2 ,2 -triflouroethanol (TFE ) . We report here amyloid fibril formation for these proteins as a function of pH . The pH at maximal fibril formation correlates with the pH dependence of protein solubility , but not with stability , for these variants . Additionally , we show that the pH at maximal fibril formation for a number of ivwell -characterized proteins is near the pI , where the protein is expected to be the least soluble . This suggests that protein solubility is an important determinant of fibril formation . en_US
dc.format.extent 6818349 bytes
dc.format.medium electronic en_US
dc.format.mimetype application /pdf
dc.language.iso en _US en_US
dc.publisher Texas A &M University en_US
dc.subject protien folding en_US
dc.title Biophysical characterization of protein folding and misfolding . en_US
dc.type Book en
dc.type.genre Electronic Dissertation en_US
dc.type.material text en_US
dc.format.digitalOrigin born digital en_US

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Biophysical characterization of protein folding and misfolding.. Available electronically from http : / /hdl .handle .net /1969 .1 /46 .

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