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Investigation of α‐keratin intermediate filament structure by molecular dynamic simulation
Author(s) -
Knopp Birgitta,
Jung Bemd,
Wortmann FranzJosef
Publication year - 1996
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.19961020122
Subject(s) - molecular dynamics , crystallography , protein filament , protein secondary structure , monomer , denaturation (fissile materials) , force field (fiction) , materials science , hydrogen bond , helix (gastropod) , chemistry , axial symmetry , molecule , computational chemistry , physics , polymer , geometry , mathematics , ecology , biochemistry , organic chemistry , quantum mechanics , biology , snail , composite material , nuclear chemistry
Molecular dynamic simulations are carried out in order to investigate the stability of the secondary and tertiary structure of the intermediate filaments monomer unit of wool. Based on the assumed secondary structure three segments of the primary structure are selected: 1A, L1,2 and a part of 2B. With the ideal α‐helix as start conformation, the simulations are carried out with the MD‐algorithm of DISCOVER 2.9.0 (BIOSYM, 1993) and the CFF91 force field for 500 ps at different temperatures in vacuum. In either simulation a destabilization of the helical structure with an increase of the simulation temperature is observed. By monitoring the length distribution of the axially oriented (O···H)‐hydrogen bonds, which stabilize the helical structure, transition temperatures for the α‐helical denaturation are determined. The supposedly α‐helical segments 1A and 2B show significantly higher transition temperatures than segment L1,2. This lower temperature confirms the expectation from the amino acid sequence that the linker segment shows more conformational flexibility and is nonhelical at room temperature.