Mesoscopic modeling of protein conformational changes
Balsera, Manuel-Angel
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https://hdl.handle.net/2142/30806
Description
Title
Mesoscopic modeling of protein conformational changes
Author(s)
Balsera, Manuel-Angel
Issue Date
1998
Doctoral Committee Chair(s)
Oono, Yoshitsugu
Department of Study
Physics
Discipline
Physics
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
protein folding, peptides, physics
Language
en
Abstract
"The conformational changes of proteins are studied theoretically with the help of coarsegrained mesoscopic models of protein structure. The models explicitly incorporate the effects of the polarity of the peptide backbone and of the specificity of hydrophobic interactions. These two features are found essential to give a realistic phase diagram of a coiled-coil peptide
without producing spurious hydrophobically collapsed ""molten-globule"" states. The model
is simple enough to allow the computational simulation of protein folding events occurring in millisecond time scales. We use the model to analyze the behavior of proteins under the perturbation due to external forces. Force induced folding/refolding transitions show a
significant hysteresis in the millisecond time scale. We find that, in general, proteins do not deform continuously as elastic bodies do, but exhibit abrupt unfolding transitions, instead."
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