2000/11/05 by Anders Irbäck, Fredrik Sjunnesson, Stefan Wallin
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · Physics and Astronomy · #Amino acid #Biochemistry #Biology #Bundle #Chemistry #Crystallography #Enzyme Structure and Function #Folding (DSP implementation) #Helix (gastropod) #Helix bundle #Hydrogen bond #Materials science #Molecule #Native state #Protein Structure and Dynamics #Protein folding #Protein structure #RNA and protein synthesis mechanisms #Ramachandran plot #cond-mat.soft #cond-mat.stat-mech #q-bio.BM
paper · pdf · doi:10.1073/pnas.240245297
published as Proc. Natl. Acad. Sci. USA 97 (2000) 13614-13618 · 15 pages, 7 figures
arxiv created 2000/11/05 · openalex publication_date 2000/11/28 · arxiv updated 2009/11/30 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05
We study the thermodynamic behavior of a model protein with 54 amino acids that forms a three-helix bundle in its native state. The model contains three types of amino acids and five to six atoms per amino acid and has the Ramachandran torsional angles phi(i), psi(i) as its degrees of freedom. The force field is based on hydrogen bonds and effective hydrophobicity forces. For a suitable choice of the relative strength of these interactions, we find that the three-helix-bundle protein undergoes an abrupt folding transition from an expanded state to the native state. Also shown is that the corresponding one- and two-helix segments are less stable than the three-helix sequence.