PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
Tytuł artykułu

The identification and the elimination of clashes in the structure of an early-stage intermediate in the protein folding process

Autorzy
Identyfikatory
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
The model (under consideration) to simulate the protein folding process assumes two steps: early stage (ES) and late stage (LS). The first is assumed to define the preliminary structure, which when applied to an optimization procedure, may produce the proper structure of the protein. However, the ES model produces the structures with clashes. This work demonstrates the possible solution to remove clashes before proceeding to the LS. Additionally, the presented solution describes mathematically the precession phenomenon, which might be useful in other fields of studies aside from protein folding such as medical imaging, quantum physics, and astronomy.
Rocznik
Strony
199--207
Opis fizyczny
Bibliogr. 11 poz., rys., wykr.
Twórcy
autor
  • Faculty of Biochemistry, Biophysics and Biotechnology, Department of Physical Biochemistry, Jagiellonian University, Gronostajowa 7, 30-387 Cracow, Poland
  • Faculty of Physics and Applied Computer Science, AGH University of Science and Technology, 30 Mickiewicza Avenue, 30-059 Cracow, Poland
Bibliografia
  • 1. Roterman I. Modelling the optimal simulation path in the peptide chain folding - studies based on geometry of alanine heptapeptide. J Theor Biol 1995;177:283-8.
  • 2. Bryliński M, Konieczny L, Czerwonko P, Jurkowski W, Roterman I. Early-stage folding in proteins (in silico) sequence-to-structure relation. J Biomed Biotechnol 2OO5;2:65-79.
  • 3. Bryliński M, Konieczny L, Kononowicz A, Roterman I. Conservative secondary structure motifs already present in early-stage folding (in silico) as found in the serpine family. J Theor Biol 2008;25l(2):275-85.
  • 4. Konieczny L, Bryliński M, Roterman I. Gauss-function-based model of hydrophobicity density in proteins. In Silico Biol 2006;6:15-22.
  • 5. Kauzmann W. Some factors in the interpretation of protein denaturation. Adv Protein Chem 1959;14:l-63.
  • 6. Roterman I, Konieczny L, Jurkowski W, Prymula K, Banach M. Two-intermediate model to characterize the structure of fast-folding proteins. J Theor Biol 2011;283:60-70.
  • 7. Kalinowska B, Alejster P, Sapała K, Baster Z, Roterman I. Hypothetical in silico model of the early-stage intermediate in protein folding. J Mol Model 2013;19:4259-69.
  • 8. Zhou AQ, O'Hern CS, Regan L. Revisiting the Ramachandran plot from a new angle. Prot Sci 2011;20:1166-71.
  • 9. Baster Z. The identification and the elimination of clashes in the structure of an early-stage intermediate in the protein folding process. Master's thesis. Cracow: AGH University of Science and Technology, 2013. Available at: http://www.zbaster.com/mastersthesisbaster.pdf. Accessed on28Oct2013.
  • 10. Richardson JS. Wikipedia, 2011 May 17. Available at: http://upload.wikimedia.org/wikipedia/commons/archive/c/cO/20130810000006%21Protein_backbone_PhiPsiOmega_drawing.jpg. Accessed on 23 July 2013.
  • 11. Urutseg, Herbye, Sulzer H. Wikipedia, 2012 May 14. Available at: http://upload.wikimedia.Org/wikipedia/commons/b/bb/Praezession.svg. Accessed on 14 July 2013.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-66a62e52-676a-4d1c-9e73-58a5c16e47ba
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.