Dynamic Monte Carlo study of the folding of a six-stranded Greek key globular protein.

Content Provider	Semantic Scholar
Author	Skolnick, Jeffrey Kolinski, Andrzej Yaris, R.
Copyright Year	1989
Abstract	To help elucidate the general rules of equilibrium globular protein folding, dynamic Monte Carlo simulations of a model beta-barrel globular protein having the six-stranded Greek key motif characteristic of real globular proteins were undertaken. The model protein possesses a typical beta-barrel amino acid sequence; however, all residues of a given type (e.g. hydrophobic residues) are identical. Even in the absence of site-specific interactions, starting from a high-temperature denatured state, these models undergo an all-or-none transition to a structurally unique six-stranded beta-barrel. These simulations suggest that the general rules of globular protein folding are rather robust in that the overall tertiary structure is determined by the general pattern of hydrophobic, hydrophilic, and turn-type residues, with site-specific interactions mainly involved in structural fine tuning of a given topology. Finally, these studies suggest that loops may play an important role in producing a unique native state. Depending on the stability of the native conformation of the long loop in the Greek key, the conformational transition can be described by a two-state, three-state, or even larger number of multiple equilibrium states model.
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://cssb.biology.gatech.edu/skolnick/publications/pdffiles/074.pdf
PubMed reference number	2919171v1
Volume Number	86
Issue Number	4
Journal	Proceedings of the National Academy of Sciences of the United States of America
Language	English
Access Restriction	Open
Subject Keyword	Amino Acid Sequence Amino Acids Anatomy, Regional Equilibrium Large Leucaena pulverulenta Protein Domain Rule (guideline) globular protein protein folding tertiary
Content Type	Text
Resource Type	Article