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http://hdl.handle.net/10603/318348
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DC Field | Value | Language |
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dc.coverage.spatial | ||
dc.date.accessioned | 2021-03-15T07:14:09Z | - |
dc.date.available | 2021-03-15T07:14:09Z | - |
dc.identifier.uri | http://hdl.handle.net/10603/318348 | - |
dc.description.abstract | In chapter 3, the effects of urea and alkylureas were investigated on thermodynamic stability and internal dynamics of heme proteins (Cyt c and Mb). To determine the effects of urea and alkylureas on the internal dynamics of heme proteins, the kinetic and thermodynamic parameters for CO-association reaction of Ferrocyt c and CO-replacement reaction of MbCO by hexacyanoferrate ion were measured under varying concentrations of urea and alkylureas (MU, DMU, EU, TMU) at pH 7.0. As [denaturant] is increased, the rate coefficient of CO-association for Ferrocyt c ( k ass ) first decrease in subdenaturing region and then increase on going from subdenaturing to denaturing milieu, which indicates that the low concentrations of denaturants constrain the internal dynamics of Ferrocyt c . Within the subdenaturing limit, the denaturant-mediated constrained dynamics of Ferrocyt c is found to be more for urea and least for TMU. However, within the subdenaturing limit, such denaturant-mediated constrained dynamics is not observed for Mb. Intermolecular docking between horse Cyt c and denaturant molecule (urea, MU, DMU, EU and TMU) reveals that polyfunctional interactions between the denaturant and different groups of and#937;-loop of Cyt c and other part of protein decrease with an increase of alkyl group on urea molecule, which suggests that the decrease in the extent of restricted dynamics of and#937;-loop with a corresponding increase of alkyl groups on urea molecule is due to the decrease of denaturant-mediated cross-linking interactions. These denaturant mediated interactions are expected to reduce the entropy of Ferrocyt c . Analysis of rate temperature data shows a progressive decrease in entropy of Ferrocyt c in the native to subdenaturing region. | |
dc.format.extent | 204p. | |
dc.language | English | |
dc.relation | ||
dc.rights | university | |
dc.title | Modulating Protein Stability and Dynamics by Osmolytes and Electrolytes | |
dc.title.alternative | ||
dc.creator.researcher | Kumar, Sandeep | |
dc.subject.keyword | Bioinorganic | |
dc.subject.keyword | Biophysical | |
dc.subject.keyword | Protein | |
dc.description.note | ||
dc.contributor.guide | Kumar, Rajesh | |
dc.publisher.place | Patiala | |
dc.publisher.university | Thapar Institute of Engineering and Technology | |
dc.publisher.institution | School of Chemistry and Biochemistry | |
dc.date.registered | ||
dc.date.completed | 2016 | |
dc.date.awarded | ||
dc.format.dimensions | ||
dc.format.accompanyingmaterial | None | |
dc.source.university | University | |
dc.type.degree | Ph.D. | |
Appears in Departments: | School of Chemistry and Biochemistry |
Files in This Item:
File | Description | Size | Format | |
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01_title.pdf | Attached File | 319.39 kB | Adobe PDF | View/Open |
02_acknowledgement.pdf | 299.87 kB | Adobe PDF | View/Open | |
03_candidates declaration.pdf | 137.08 kB | Adobe PDF | View/Open | |
04_list of abbreviations.pdf | 409.72 kB | Adobe PDF | View/Open | |
05_contents.pdf | 420.41 kB | Adobe PDF | View/Open | |
06_abstract.pdf | 423.17 kB | Adobe PDF | View/Open | |
07_chapter 1.pdf | 918.15 kB | Adobe PDF | View/Open | |
08_chapter 2.pdf | 785.07 kB | Adobe PDF | View/Open | |
09_chapter 3.pdf | 1.95 MB | Adobe PDF | View/Open | |
10_chapter 4.pdf | 1.2 MB | Adobe PDF | View/Open | |
11_chapter 5.pdf | 1.23 MB | Adobe PDF | View/Open | |
12_chapter 6.pdf | 1.21 MB | Adobe PDF | View/Open | |
13_chapter 7.pdf | 1.73 MB | Adobe PDF | View/Open | |
14_chapter 8.pdf | 1.1 MB | Adobe PDF | View/Open | |
15_appendix.pdf | 502.53 kB | Adobe PDF | View/Open | |
16_list of publications.pdf | 702.57 kB | Adobe PDF | View/Open | |
80_recommendation.pdf | 1.45 MB | Adobe PDF | View/Open |
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