M. Beck

Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin II: a Fourier-transform infrared spectroscopy study of site-directed mutants.

K. Fahmy, T. Sakmar, F. Jäger, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Spectroscopic evidence for interaction between transmembrane helices 3 and 5 in rhodopsin.

T. Sakmar, F. Siebert, M. Beck, 1998, Biochemistry.

Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition.

T. Sakmar, T. Zvyaga, K. Min, 1993, The Journal of biological chemistry.

Evidence for the specific interaction of a lipid molecule with rhodopsin which is altered in the transition to the active state metarhodopsin II 1

T. Sakmar, F. Siebert, M. Beck, 1998, FEBS letters.

The role of Glu181 in the photoactivation of rhodopsin.

Steffen Lüdeke, T. Sakmar, R. Vogel, 2005, Journal of molecular biology.

FTIR Investigations of Rhodopsin and Rhodopsin Mutants in Detergent and Reconstituted into Membranes

T. Sakmar, F. Siebert, M. Beck, 1995 .

Interaction Between His211 and Glu122 in Rhodopsin: an FT-IR Study of Rhodopsin and Site-Directed Mutants

T. Sakmar, F. Siebert, M. Beck, 1997 .