Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Ilona L. Canestrelli"'
Autor:
Ilona L. Canestrelli, Ulrich K. Genick, G. Tollin, Savitha Devanathan, Michael A. Cusanovich, Terry E. Meyer, Elizabeth D. Getzoff
Publikováno v:
Biochemistry. 37:11563-11568
There are previously two known intermediates (I1 and I2) in the room-temperature photocycle of the photoactive yellow protein (PYP) from Ectothiorhodospira halophila. The three-dimensional structures of ground-state PYP and of I2 have shown that ligh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12c844e594d42c047c10dbd8fc27e79a
https://doi.org/10.1021/bi9803776
https://doi.org/10.1021/bi9803776
Publikováno v:
Nature. 392:206-209
Protein photosensors from all kingdoms of life use bound organic molecules, known as chromophores, to detect light. A specific double bond within each chromophore is isomerized by light, triggering slower changes in the protein as a whole. The initia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bcb6673a2b6361e99dd0c256e9589ca
https://doi.org/10.1038/32462
https://doi.org/10.1038/32462
Autor:
Ilona L. Canestrelli, Savitha Devanathan, Erica Williams, Elizabeth D. Getzoff, Ulrich K. Genick, G. Tollin, Michael A. Cusanovich, Terry E. Meyer
Publikováno v:
Biochemistry. 36:8-14
To understand how the protein and chromophore components of a light-sensing protein interact to create a light cycle, we performed time-resolved spectroscopy on site-directed mutants of photoactive yellow protein (PYP). Recently determined crystallog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8a59013172ef23f15894ec03e1bf534
https://doi.org/10.1021/bi9622884
https://doi.org/10.1021/bi9622884
Autor:
Victoria A. Roberts, Ilona L. Canestrelli, Jon D. Stewart, Stephen J. Benkovic, Elizabeth D. Getzoff, Andrew S. Arvai, Eric H. Olender, Maria M. Thayer, Cami K. Koike
Publikováno v:
Journal of molecular biology. 291(2)
Among catalytic antibodies, the well-characterized antibody 43C9 is unique in its ability to catalyze the difficult, but desirable, reaction of selective amide hydrolysis. The crystallographic structures that we present here for the single-chain vari
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::256f8d8c37a2d31039f72581af24e2a8
https://pubmed.ncbi.nlm.nih.gov/10438624
https://pubmed.ncbi.nlm.nih.gov/10438624