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https://hdl.handle.net/20.500.12202/4092
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DC Field | Value | Language |
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dc.contributor.author | Berger, Jacob | |
dc.date.accessioned | 2018-11-06T18:28:57Z | |
dc.date.available | 2018-11-06T18:28:57Z | |
dc.date.issued | 2011-05 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12202/4092 | |
dc.identifier.uri | https://ezproxy.yu.edu/login?url=https://repository.yu.edu/handle/20.500.12202/4092 | |
dc.description | The file is restricted for YU community access only. | |
dc.description.abstract | Protein crystallization has been studied for over 150 years but is still not well understood. Protein crystals are extremely difficult to grow since protein crystallization is sensitive to many parameters. In this thesis I investigate if the chirality of a precipitant, 2- methyl-2,4-pentanediol (MPD), influences the crystal growth of the protein lysozyme. It appears that R-MPD has a single conformation within the crystal, while S-MPD may take on a few different conformations. Although there appears to be a chiral difference within the structure, this does not seem to dramatically affect the kinetics of crystal growth as both crystal structures form in the same period of time. | en_US |
dc.description.sponsorship | Jay and Jeanie Schottenstein Honors Program | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | Yeshiva College | en_US |
dc.rights | Attribution-NonCommercial-NoDerivs 3.0 United States | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/us/ | * |
dc.subject | Lysozyme. | en_US |
dc.subject | Proteins --Structure. | en_US |
dc.subject | Proteins --Synthesis. | en_US |
dc.title | The Effect of Precipitant Chirality on the Crystallization of Lysozyme | en_US |
dc.type | Thesis | en_US |
Appears in Collections: | Jay and Jeanie Schottenstein Honors Student Theses |
Files in This Item:
File | Description | Size | Format | |
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Jacob-Berger.pdf Restricted Access | 1.34 MB | Adobe PDF | View/Open |
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