Equilibrium and Kinetic folding properties of alpha-helical Greek key protein domains
| dc.contributor.advisor | Carla Mattos, Committee Member | en_US |
| dc.contributor.advisor | A. Clay Clark, Committee Chair | en_US |
| dc.contributor.advisor | Harold Swaisgood, Committee Member | en_US |
| dc.contributor.advisor | Dennis T. Brown, Committee Member | en_US |
| dc.contributor.author | Chen, Yun-Ru | en_US |
| dc.date.accessioned | 2010-04-02T18:35:14Z | |
| dc.date.available | 2010-04-02T18:35:14Z | |
| dc.date.issued | 2003-11-13 | en_US |
| dc.degree.discipline | Biochemistry | en_US |
| dc.degree.level | dissertation | en_US |
| dc.degree.name | PhD | en_US |
| dc.description.abstract | I have characterized the equilibrium and kinetic folding properties of members of alpha-helical Greek key protein domain, caspase recruitment domains of RICK (RICK-CARD) and procaspase-1 (Pro-1-CARD). At equilibrium, folding of both RICK-CARD and Pro-1-CARD is well described by a two-state mechanism representing the native and unfolded ensembles. The proteins are marginally stable,with the Gibbs free energy of 3.0 and 1.1 kcal/mol and m-values of 1.27 and 0.68 kcal/mol/M for RICK-CARD and Pro-1-CARD, respectively (30 mM Tris-HCl, pH 8, 1 mM DTT, 25 degree Celsius). The folding pathways of RICK-CARD are complex and contain at least two or three non-native conformations. The major folding event of RICK-CARD has a folding rate constant of 30 s⁻¹. Studies on seven mutants of RICK-CARD suggest that the three prolyl residues contribute to its structural stability and folding complexity. The folding of Pro-1-CARD is different than that of RICK-CARD. The folding and unfolding kinetics of Pro-1-CARD are fast but with kinetically trapped intermediates present, which appear to be similar to that of RICK-CARD. The work suggests that different alpha-helical Greek key protein domains fold differently but may share some similar folding pathways. | en_US |
| dc.identifier.other | etd-10282003-162718 | en_US |
| dc.identifier.uri | http://www.lib.ncsu.edu/resolver/1840.16/3718 | |
| dc.rights | I hereby certify that, if appropriate, I have obtained and attached hereto a written permission statement from the owner(s) of each third party copyrighted matter to be included in my thesis, dissertation, or project report, allowing distribution as specified below. I certify that the version I submitted is the same as that approved by my advisory committee. I hereby grant to NC State University or its agents the non-exclusive license to archive and make accessible, under the conditions specified below, my thesis, dissertation, or project report in whole or in part in all forms of media, now or hereafter known. I retain all other ownership rights to the copyright of the thesis, dissertation or project report. I also retain the right to use in future works (such as articles or books) all or part of this thesis, dissertation, or project report. | en_US |
| dc.subject | protein folding | en_US |
| dc.subject | alpha helical Greek key | en_US |
| dc.subject | caspase recruitment domains | en_US |
| dc.title | Equilibrium and Kinetic folding properties of alpha-helical Greek key protein domains | en_US |
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