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Thermal folding and mechanical unfolding pathways of protein secondary structures
Author(s) -
Cieplak Marek,
Hoang Trinh Xuan,
Robbins Mark O.
Publication year - 2002
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.10188
Subject(s) - folding (dsp implementation) , stiffness , molecular dynamics , protein secondary structure , helix (gastropod) , protein folding , tandem , alpha helix , displacement (psychology) , crystallography , biophysics , thermal , contact order , chemistry , chemical physics , physics , materials science , thermodynamics , computational chemistry , biology , circular dichroism , structural engineering , biochemistry , ecology , psychology , snail , engineering , composite material , psychotherapist
Mechanical stretching of secondary structures is studied through molecular dynamics simulations of a Go‐like model. Force versus displacement curves are studied as a function of the stiffness and velocity of the pulling device. The succession of stretching events, as measured by the order in which contacts are ruptured, is compared to the sequencing of events during thermal folding and unfolding. Opposite cross‐correlations are found for an α‐helix and a β‐hairpin structure. In a tandem of two α‐helices, the two constituent helices unravel nearly simultaneously. A simple condition for simultaneous versus sequential unraveling of repeat units is presented. Proteins 2002;49:104–113. © 2002 Wiley‐Liss, Inc.