Short-time dynamics of the helix-coil transition in polypeptides.
We study the critical relaxation of the helix-coil transition in all-atom models of polyalanine chains. We show that at the critical temperature the decay of a completely helical conformation can be described by scaling relations that allow us estimating the pertinent critical exponents. The present approach opens a new way for characterizing transitions in proteins and may lead to a better understanding of their folding mechanism. An application of the technique to the 34-residue human parathyroid fragment PTH(1-34) supports universality of the helix-coil transition in homopolymers and (helical) proteins.
Arashiro
Everaldo
E
Departamento de Física e Matemática, FFCLRP Universidade de São Paulo, Avenida Bandeirantes 3900, CEP 14040-901, Ribeirão Preto, São Paulo, Brazil. everaldo@pg.ffclrp.usp.br
Drugowich de Felício
J R
JR
Hansmann
Ulrich H E
UH
D003198:Computer Simulation; D006801:Humans; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D009038:Motion; D010446:Peptide Fragments / Q000737:chemistry* / Q000648:ultrastructure*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D019379:Teriparatide / Q000031:analogs & derivatives* / Q000737:chemistry
D010446:Peptide Fragments; D010455:Peptides; D019379:Teriparatide; C035748:parathyroid hormone (1-34)amide