Mesoscopic modeling of protein conformational changes

"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."

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Physics

Year dc:date

2012

Author dc:creator

• Balsera, Manuel-Angel

Contributors dc:contributor

• Oono, Yoshitsugu

• protein folding, peptides, physics

Statement dc:rights

• ©1998 Manuel-Angel Balsera

Language dc:language

en

Identifier

4224054

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/30806