Files in this item

FilesDescriptionFormat

application/pdf

application/pdf1998_balsera.pdf (6MB)Restricted to U of Illinois
1998_balseraPDF

Description

Title:Mesoscopic modeling of protein conformational changes
Author(s):Balsera, Manuel-Angel
Doctoral Committee Chair(s):Oono, Yoshitsugu
Department / Program:Physics
Discipline:Physics
Degree:Ph.D.
Genre:Dissertation
Subject(s):protein folding, peptides, physics
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.
Issue Date:1998
Genre:Dissertation / Thesis
Type:Text
Language:English
URI:http://hdl.handle.net/2142/30806
Rights Information:©1998 Manuel-Angel Balsera
Date Available in IDEALS:2012-05-05
Identifier in Online Catalog:4224054


This item appears in the following Collection(s)

Item Statistics