2002/01/21 by Josh P. Kemp, Jeff Z. Y. Chen, J. Z. Y Chen
Biochemistry, Genetics and Molecular Biology · Chemistry · Engineering · Materials Science · Mathematics · Physics and Astronomy · #Biochemistry #Biology #Biophysics #Chemical physics #Chemistry #Computational chemistry #Crystallography #Downhill folding #Engineering #Enzyme Structure and Function #Folding (DSP implementation) #Helix (gastropod) #Mathematics #Molecular dynamics #Monte Carlo method #Nucleation #Phi value analysis #Physics #Protein Structure and Dynamics #Protein folding #Protein secondary structure #RNA and protein synthesis mechanisms #Sequence (biology) #Thermodynamics #cond-mat.soft #cond-mat.stat-mech #q-bio
paper · pdf · doi:10.1209/epl/i2002-00185-0
published as Revised version can be seen: Europhys Lett 59, 721 (2002) · 3 figures Submitted to Europhys Letter
arxiv created 2002/01/21 · openalex publication_date 2002/09/01 · openalex created_date 2016/06/24 · arxiv updated 2016/08/31 · openalex updated_date 2026/08/05
The folding of a polypeptide is associated with the formation of domain structures that have the form of α-helix or β-sheet. Of biological importance is how a secondary structure, such as an α-helix, spontaneously forms during the collapse of a peptide from an initial denatured state. The Monte Carlo implementation of a recent helix-forming model enables us to study the entire folding process dynamically. As shown by our computer simulations, the foldability and helical propagation are both strongly correlated to the nucleation properties of a given residue sequence.