α-Helix and β-Hairpin Folding from Experiment, Analytical Theory and Molecular Dynamics Simulations

Title: α-Helix and β-Hairpin Folding from Experiment, Analytical Theory and Molecular Dynamics Simulations

Volume: 3 Issue: 2

Author(s): Oxana V. Galzitskaya, Junichi Higo and Alexei V. Finkelstein

Affiliation:

Keywords: helix, hairpin, peptide folding

Abstract: The α-helix and β-hairpin are the minimal secondary structure elements of proteins. Identification of the factors governing the formation of these structures independently of the rest of the protein is important for understanding the determinants and rules driving the folding process to a unique native structure. It has been shown that some α-helices and β-hairpins can fold autonomously into native-like structures, either in aqueous solution or in the presence of an organic co-solvent possible mechanisms of these processes have been considered in literature. The characteristic times for folding of α and β structures are estimated from experiments, simple analytical theories and more detailed computer models. Our aim is to review recent experimental and theoretical studies of folding of α and β structures focusing much attention on β-hairpins.

Cite this article as:

Galzitskaya V. Oxana, Higo Junichi and Finkelstein V. Alexei, α-Helix and β-Hairpin Folding from Experiment, Analytical Theory and Molecular Dynamics Simulations, Current Protein & Peptide Science 2002; 3 (2) . https://dx.doi.org/10.2174/1389203024605340