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dc.contributor.advisor Fernandez, Ariel
dc.creatorChen, Jianping
dc.date.accessioned 2018-12-03T18:32:05Z
dc.date.available 2018-12-03T18:32:05Z
dc.date.issued 2008
dc.identifier.urihttps://hdl.handle.net/1911/103640
dc.description.abstract Hydrogen bond plays an important role in stability, dynamics and function of protein. Most of backbone hydrogen bonds are well wrapped by nonpolar groups of side chains. However, there are a small portion of hydrogen bonds vulnerable to water attack. Those under-wrapped hydrogen bonds, termed as "dehydron", are sensitive to the change in the local electrostatic environment. Dehydrons constitute a hot spot for protein interactions. They have been identified as structural marker for protein association, proteamic connectivity and protein-ligand binding. The effects of dehydrons on protein hydration shell are assessed by studying the mobility of hydration water. Calculation of water residence times of all residues reveals that dehydrons enhance the water mobility and promote the most intense loosening of hydration shell. Targeting loose hydration shells induced by dehydrons provides a powerful strategy in rational drug design.
dc.format.extent 60 pp
dc.language.iso eng
dc.subjectBiomedical research
Biophysics
Applied sciences
Biological sciences
dc.title Protein wrapping and protein hydration
dc.identifier.digital 304532925
dc.type.genre Thesis
dc.type.material Text
thesis.degree.department Physics
thesis.degree.discipline Natural Sciences
thesis.degree.grantor Rice University
thesis.degree.level Masters
thesis.degree.name Master of Science
dc.identifier.callno THESIS PHYS. 2008 CHEN
dc.identifier.citation Chen, Jianping. "Protein wrapping and protein hydration." (2008) Master’s Thesis, Rice University. https://hdl.handle.net/1911/103640.


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