Generalized-ensemble simulations of the human parathyroid hormone fragment PTH(1-34)

2003/10/23 by Ulrich H. E. Hansmann
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · Physics and Astronomy · #Enzyme Structure and Function #Mass Spectrometry Techniques and Applications #Protein Structure and Dynamics #cond-mat.dis-nn #cond-mat.stat-mech #physics.bio-ph #q-bio.BM

paper · pdf · doi:10.1063/1.1630563

To appear in J. Chem. Phys

arxiv created 2003/10/23 · openalex publication_date 2003/12/22 · arxiv updated 2009/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01

Abstract

A generalized-ensemble technique, multicanonical sampling, is used to study the folding of a 34-residue human parathyroid hormone fragment. An all-atom model of the peptide is employed and the protein-solvent interactions are approximated by an implicit solvent. Our results demonstrate that generalized-ensemble simulations are well suited to sample low-energy structures of such large polypeptides. Configurations with a root-mean-square deviation to the crystal structure of less than 1 A are found. Finally, we discuss limitations of our implicit solvent model.

Citations

• The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies