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Helical Nature of Collective Excitations in α‐Helical Protein
Author(s) -
Ichinose S.
Publication year - 1991
Publication title -
physica status solidi (b)
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.51
H-Index - 109
eISSN - 1521-3951
pISSN - 0370-1972
DOI - 10.1002/pssb.2221650208
Subject(s) - collective motion , quasiparticle , resonance (particle physics) , peptide , radius , helix (gastropod) , physics , molecule , motion (physics) , molecular physics , condensed matter physics , crystallography , chemistry , atomic physics , classical mechanics , nuclear magnetic resonance , quantum mechanics , biology , computer science , ecology , superconductivity , snail , computer security
Collective excitations in long α‐helical proteins are investigated, including two types of peptide groups displacements provided by changes of the helix pitch and its radius. It is shown that the motion of asymmetric excitations along the protein molecule have a helical nature. For these excitations there occurs an exchange of excitations between chains as a result of the resonance interaction between peptide groups belonging to different chains.