ATP-Induced Transconformation of Myosin Revealed by Determining Three-Dimensional Positions of Fluorophores from Fluorescence Energy Transfer Measurements

2000 ◽  
Vol 132 (1) ◽  
pp. 6-18 ◽  
Author(s):  
Takuo Yasunaga ◽  
Yoshikazu Suzuki ◽  
Reiko Ohkura ◽  
Kazuo Sutoh ◽  
Takeyuki Wakabayashi
1983 ◽  
Vol 215 (2) ◽  
pp. 413-416 ◽  
Author(s):  
N C Genov ◽  
M Shopova ◽  
R Boteva ◽  
F Ricchelli ◽  
G Jori

Singlet-singlet energy transfer from the tryptophan residues to an active-site-serine-bound 5-dimethylaminonaphthalene-1-sulphonyl group was investigated in four subtilisins. The transfer distances for subtilisin Novo and mesentericopeptidase are 1.93 +/- 0.20 nm (19.3 +/- 2.0 A) and 1.81 +/- 0.20 nm (18.1 +/- 2.0 A) respectively. The positions of the indole groups in the three-dimensional structures of the two pairs of proteinases, namely subtilisin Novo and mesentericopeptidase on the one hand and subtilisins Carlsberg and DY on the other, are essentially identical.


2000 ◽  
Vol 280 (2) ◽  
pp. 272-277 ◽  
Author(s):  
Bernhard Oswald ◽  
Frank Lehmann ◽  
Lydia Simon ◽  
Ewald Terpetschnig ◽  
Otto S. Wolfbeis

2013 ◽  
Vol 8 (1) ◽  
pp. 452 ◽  
Author(s):  
Yulia A Gromova ◽  
Anna O Orlova ◽  
Vladimir G Maslov ◽  
Anatoly V Fedorov ◽  
Alexander V Baranov

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