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2001 | 48 | 1 | 77-81
Article title

Monte Carlo simulations of protein-like heteropolymers.

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EN
Abstracts
EN
Properties of a simple model of polypeptide chains were studied by the means of the Monte Carlo method. The chains were built on the (310) hybrid lattice. The residues interacted with long-range potential. There were two kinds of residues: hydrophobic and hydrophilic forming a typical helical pattern -HHPPHPP-. Short range potential was used to prefer helical conformations of the chain. It was found that at low temperatures the model chain formes dense and partially ordered structures (non-unique). The presence of the local potential led to an increase of helicity. The effect of the interplay between the two potentials was studied. After the collapse of the chain further annealing caused rearrangement of helical structures. Dynamic properties of the chain at low temperature depended strongly on the local chain ordering.
Publisher

Year
Volume
48
Issue
1
Pages
77-81
Physical description
Dates
published
2001
received
2000-10-6
revised
2000-12-23
accepted
2001-02-12
Contributors
  • Department of Chemistry, University of Warsaw, Warszawa, Poland
  • Department of Chemistry, University of Warsaw, Warszawa, Poland
References
  • 1. Anfinsen, C.B. (1973) Principles that govern the folding of protein chains. Science 181, 223-230.
  • 2. Dill, K.A., Bromberg, S., Yue, K., Fiebig, K.M., Yee, D.P., Thomas, P.D. & Chan, H.S. (1995) Principles of protein folding A perspective from simple exact models. Protein Sci. 4, 561-602.
  • 3. Sikorski, A. & Skolnick, J. (1989) Monte Carlo studies on equilibrium globular protein folding. III. The four helix bundle. Biopolymers 28, 1097-1113.
  • 4. Sikorski, A. & Skolnick, J. (1989) Monte Carlo simulation of equilibrium globular folding. alpha-Helical bundles with long loops. Proc. Natl. Acad. Sci. U.S.A. 86, 2668-2672.
  • 5. Sikorski, A. & Skolnick, J. (1990) Dynamic Monte Carlo simulations of globular protein folding/unfolding pathways. II. alpha-Helical motifs. J. Mol. Biol. 212, 819-836.
  • 6. Kolinski, A. & Madziar, P. (1997) Collapse transition in protein-like lattice polymers: The effect of sequence patterns. Biopolymers 42, 537-548.
  • 7. Romiszowski, P. & Sikorski, A. (1999) A Monte Carlo study of properties of protein-like heteropolymers. Physica A. 273, 190-197.
  • 8. Romiszowski, P. & Sikorski, A. (2000) The influence of sequence patterns and local conformational preferences on the structure of collapsed polypeptide. Biopolymers 54, 262-272.
  • 9. Kolinski, A. & Skolnick, J. (1993) Monte Carlo simulation of protein folding. I. Lattice model and interaction scheme. Proteins 18, 338-352.
  • 10. Kolinski, A. & Skolnick, J. (1997) High coordination lattice models of protein structure, dynamics and thermodynamics. Acta Biochim. Polon. 44, 389-422.
  • 11. Nishikawa, K., Momany, F.A. & Scheraga, H.A. (1974) Low-energy structures of two dipeptides and their relation to bend conformations. Macromolecules 7, 797-805.
  • 12. Kolinski, A., Milik, M., Rycombel, J. & Skolnick, J. (1995) A reduced model of short range interactions in polypeptide chain. J. Chem. Phys. 103, 4312- 4323.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv48i1p77kz
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