α-Helix structure of parathyroid hormone fragment (1-34) predicted by Monte Carlo simulated annealing
- 12 January 2009
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 42 (3), 300-303
- https://doi.org/10.1111/j.1399-3011.1993.tb00146.x
Abstract
Tertiary structure of parathyroid hormone fragment (1-34) is predicted by the Monte Carlo simulated annealing method. Among the 20 structures obtained after completely unbiased calculations, the lowest-energy conformation exhibits two alpha-helices around residues 2-10 and 18-22. This structure agrees with the models, especially with the location of helices, deduced from experiments. In addition, the simulation supports empirical implications in the following two points. (1) The helix near the N-terminus is more stable than the C-terminal one. (2) The rest of the peptide segments are flexible and do not tend to have any definite structure. Our calculation correctly predicts only an alpha-helix, whereas previous analyses by the Chou-Fasman method leave an ambiguity between an alpha-helix and a beta-strand.Keywords
This publication has 15 references indexed in Scilit:
- β-sheet folding of fragment (16–36) of bovine pancreatic trypsin inhibitor as predicted by Monte Carlo simulated annealingProtein Engineering, Design and Selection, 1992
- Investigation of the solution structure of the human parathyroid hormone fragment (1-34) by proton NMR spectroscopy, distance geometry, and molecular dynamics calculationsBiochemistry, 1991
- Monte Carlo Simulated Annealing Prediction for α-Helix Propensity of Amino Acid HomopolymersChemistry Letters, 1991
- α-Helix folding by Monte Carlo simulated annealing in isolated C-peptide of ribonuclease AProtein Engineering, Design and Selection, 1991
- Applications of simulated annealing to peptidesBiopolymers, 1990
- A prediction of tertiary structures of peptide by the Monte Carlo simulated annealing methodProtein Engineering, Design and Selection, 1989
- Two‐dimensional 1H‐NMR study of the 1–34 fragment of human parathyroid hormoneBiopolymers, 1989
- Optimization by Simulated AnnealingScience, 1983
- Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acidsThe Journal of Physical Chemistry, 1983
- Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acidsThe Journal of Physical Chemistry, 1975