Skip to main content
Article thumbnail
Location of Repository

Intermediates in the Protein Folding Process: A Computational Model

By Wiktor Jurkowski, Mateusz Banach, Irena Roterman and Leszek Konieczny

Abstract

The paper presents a model for simulating the protein folding process in silico. The two-step model (which consists of the early stage—ES and the late stage—LS) is verified using two proteins, one of which is treated (according to experimental observations) as the early stage and the second as an example of the LS step. The early stage is based solely on backbone structural preferences, while the LS model takes into account the water environment, treated as an external hydrophobic force field and represented by a 3D Gauss function. The characteristics of 1ZTR (the ES intermediate, as compared with 1ENH, which is the LS intermediate) confirm the link between the gradual disappearance of ES characteristics in LS structural forms and the simultaneous emergence of LS properties in the 1ENH protein. Positive verification of ES and LS characteristics in these two proteins (1ZTR and 1ENH respectively) suggest potential applicability of the presented model to in silico protein folding simulations

Topics: protein structure, hydrophobicity, divergence entropy, intermediates in protein folding, LCC:Chemistry, LCC:QD1-999, LCC:Science, LCC:Q, DOAJ:Chemistry (General), DOAJ:Chemistry
Publisher: Molecular Diversity Preservation International
Year: 2011
DOI identifier: 10.3390/ijms11084850
OAI identifier: oai:doaj.org/article:4d8d4493d0094fac89c2b2698c9d90fe
Journal:
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • http://doaj.org/search?source=... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.