Monte Carlo simulations of proteins in cages: influence of confinement on the stability of intermediate states.

Abstract:

:We study the folding of small proteins inside confining potentials. Proteins are described using an effective potential model that contains the Ramachandran angles as degrees of freedom and does not need any a priori information about the native state. Hydrogen bonds, dipole-dipole-, and hydrophobic interactions are taken explicitly into account. An interesting feature displayed by this potential is the presence of metastable intermediates between the unfolded and native states. We consider different types of confining potentials to describe proteins folding inside cages with repulsive or attractive walls. Using the Wang-Landau algorithm, we determine the density of states and analyze in detail the thermodynamical properties of the confined proteins for different sizes of the cages. We show that confinement dramatically reduces the phase space available to the protein and that the presence of intermediate states can be controlled by varying the properties of the confining potential. Cages with strongly attractive walls destabilize the intermediate states and lead to a two-state folding into a configuration that is less stable than the native structure. However, cages with slightly attractive walls enhance the stability of native structure and induce a folding process, which occurs through intermediate configurations.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Ojeda P,Garcia ME,Londoño A,Chen NY

doi

10.1529/biophysj.107.125369

subject

Has Abstract

pub_date

2009-02-01 00:00:00

pages

1076-82

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(08)00010-6

journal_volume

96

pub_type

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