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Dijital Arşivi

Analysis of folding kinetics for simplified model proteins

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dc.contributor Ph.D. Program in Chemical Engineering.
dc.contributor.advisor Bahar, Ivet.
dc.contributor.author Özkan, Ş. Banu.
dc.date.accessioned 2023-03-16T11:13:37Z
dc.date.available 2023-03-16T11:13:37Z
dc.date.issued 2001.
dc.identifier.other CHE 2001 O85 PhD
dc.identifier.uri http://digitalarchive.boun.edu.tr/handle/123456789/14885
dc.description.abstract The conformational stochastics of simplified model chains that show an apparent two-state kinetics was explored.. A fundamental question addressed in the present analysis is to understand if the folding takes place through a continuum of paths, or if a preferred pathway involving subcooperative folding events can be discerned. To this aim, the complete sets of conformations for short model chains were generated as self-avoiding walks on a square lattice. Native-like contacts have been assigned attractive potentials, and transition rates have been assigned on the basis of native-like contacts and root-mean-square deviations between conformations. The time evolution of all conformational transitions has been analyzed starting from a uniform distribution of conformations, using a master equation formalism. A key conclusion is that: (i) The lack of intermediates that define two-state kinetics does not preclude folding through a specific sequence of events. (ii) F-value analysis, a measure of the stability and change in folding kinetics due to mutation reveals that non classical F-values can arise from parallel microscopic flow processes. Negative F values result when a mutation destabilizes a slow flow channel, causing an overflow into a faster flow channel. F-values greater than one occur when mutations redirect a fast flow into a slower channel.
dc.format.extent 30 cm.
dc.publisher Thesis (Ph.D.) - Bogazici University. Institute for Graduate Studies in Science and Engineering, 2001.
dc.subject.lcsh Protein folding.
dc.title Analysis of folding kinetics for simplified model proteins
dc.format.pages xiii, 87 leaves ;


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