Abstract
Betanova is a monomeric, three-stranded antiparallel beta-sheet protein with twenty residues. The pathways between the folded native structure and unfolded conformations of betanova are studied using UNRES force field and the most popular computer simulation method, Metropolis Monte Carlo algorithm. At a fixed temperature, 100 Monte Carlo simulations are performed, starting from the folded native structure, and the pathways are obtained at two different temperatures.
Highlights
Polypeptides are linear polymers, built of twenty different amino acids, with a defined residue sequence [1]
Information on the tertiary native structure of a protein is quite crucial in understanding its biological function and role
We study the pathways between the folded native structure and unfolded conformations of betanova using UNRES force field [3] and the most popular computer simulation method, Metropolis Monte Carlo algorithm [4]
Summary
Polypeptides are linear polymers, built of twenty different amino acids (or residues), with a defined residue sequence [1]. The linear residue sequence of a protein is called the primary structure. The popular local conformations of backbones, such as alpha-helix and beta-sheet, of proteins correspond to the secondary structure. Understanding the processes between the primary structure and the tertiary native structure is one of the most important problems in modern science. Understanding these processes is important in this post-genomic era. Its primary structure is given by Arg-Gly-Trp-Ser-Val-Gln-Asn-Gly-Lys-Tyr-Thr-Asn-Asn-Gly-Lys-Thr-Thr-Glu-Gly-Arg. In this work, we study the pathways between the folded native structure and unfolded conformations of betanova using UNRES force field [3] and the most popular computer simulation method, Metropolis Monte Carlo algorithm [4]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
