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Md‐simulation of α‐keratin intermediate filaments
Author(s) -
Knopp Birgitta,
Jung Bernd,
Wortmann FranzJosef,
Höcker Hartwig
Publication year - 1994
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.19940810139
Subject(s) - molecular dynamics , helix (gastropod) , monomer , protein filament , crystallography , materials science , hydrogen bond , linker , chemical physics , chemistry , molecule , computational chemistry , polymer , computer science , composite material , ecology , organic chemistry , snail , biology , operating system
In recent years powerful computer systems have become readily accessible to simulate complex chemical problems. Based on the primary structure of the intermediate filament monomer unit of wool, small sequences are selected. Their molecular dynamic behaviour is simulated, in order to investigate the secondary and tertiary structure as well as their stability. The simulations are carried out for a helical segment and a linker segment, selecting the ideal α‐helix as start conformation. In vacuum all simulations show an unstable α‐helix due to shifts of the intrahelical hydrogen bonds. So a new helical structure with a larger helix diameter is formed. However in simulations with surrounding water the α‐helix remains stable throughout the simulation time. Up to now it has not been possible to dectect any fundamental difference in the molecular dynamic behaviour of the helical and the linker segment.