title: Arginine52 controls the photoisomerization process in photoactive yellow protein.
authors.affiliation: Department of Theoretical and Computational Biophysics, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany. ggroenh@gwdg.de
authors.forename: Gerrit
authors.initials: G
authors.lastname: Groenhof
authors.forename: Lars V
authors.initials: LV
authors.lastname: Schäfer
authors.forename: Martial
authors.initials: M
authors.lastname: Boggio-Pasqua
authors.forename: Helmut
authors.initials: H
authors.lastname: Grubmüller
authors.forename: Michael A
authors.initials: MA
authors.lastname: Robb
mesh_terms: D001120:Arginine / Q000737:chemistry* / Q000528:radiation effects*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000528:radiation effects*; D008956:Models, Chemical; D010777:Photochemistry; D020283:Photoreceptors, Microbial / Q000737:chemistry* / Q000528:radiation effects*; D011487:Protein Conformation; D011789:Quantum Theory; D013237:Stereoisomerism; D013997:Time Factors; D014466:Ultraviolet Rays
chemical_list: D001426:Bacterial Proteins; D020283:Photoreceptors, Microbial; C050162:photoactive yellow protein, Bacteria; D001120:Arginine