caa a22 4500 386381070 CHVBK 20180307112042.0 cr unu---uuuuu 161130e198911 xx s 000 0 eng 10.1017/S0033583500003164 doi S0033583500003164 pii (NATIONALLICENCE)cambridge-10.1017/S0033583500003164 Schweitzer-Stenner Reinhard University of Bremen, Physics Department, 2800 Bremen, Federal Republic of Germany Allosteric linkage-induced distortions of the prosthetic group in haem proteins as derived by the theoretical interpretation of the depolarization ratio in resonance Raman scattering [Elektronische Daten] [Reinhard Schweitzer-Stenner] The relationship between functional properties of haem proteins, particularly ligand binding and Bohr effect, and associated variations of the tertiary and quaternary structures is one of the main objectives of haem protein research. In this context one aims to get detailed knowledge of the coupling mechanisms which are involved in the transduction of structural changes from the protein to the functional haem group along distinct pathways. Copyright © Cambridge University Press 1989 Quarterly Reviews of Biophysics Cambridge University Press 22/4(1989-11), 381-479 0033-5835 22:4<381 1989 22 QRB https://doi.org/10.1017/S0033583500003164 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1017/S0033583500003164 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Schweitzer-Stenner Reinhard University of Bremen, Physics Department, 2800 Bremen, Federal Republic of Germany NATIONALLICENCE 773 0- Quarterly Reviews of Biophysics Cambridge University Press 22/4(1989-11), 381-479 0033-5835 22:4<381 1989 22 QRB CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-cambridge