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T1  - Interaction of Biliverdin Chromophore with Near-Infrared Fluorescent Protein BphP1-FP Engineered from Bacterial Phytochrome 
SN  -  /  
UR  - http://hdl.handle.net/10138/203370 
T3  -  
A1  - Stepanenko, Olesya V.; Stepanenko, Olga V.; Kuznetsova, Irina M.; Shcherbakova, Daria M.; Verkhusha, Vladislav; Turoverov, Konstantin K. 
A2  -  
PB  -  
Y1  - 2017 
LA  - eng 
AB  - Near-infrared (NIR) fluorescent proteins (FPs) designed from PAS (Per-ARNT-Sim repeats) and GAF (cGMP phosphodiesterase/adenylate cyclase/FhlA transcriptional activator) domains of bacterial phytochromes covalently bind biliverdin (BV) chromophore via one or two Cys residues. We studied BV interaction with a series of NIR FP variants derived from the recently reported BphP1-FP protein. The latter was engineered from a bacterial phytochrome RpBphP1, and has two reactive Cys residues (Cys15 in the... 
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KW  - bacterial phytochrome; iRFP; IFP; near-infrared fluorescent protein; GAF domain; biliverdin; competitive inhibition; HISTIDINE KINASES; BACTERIOPHYTOCHROMES; BRIGHT; PHOTORECEPTOR; SIMILARITY; REVEALS; DOMAIN; AGP1; 3111 Biomedicine; 1182 Biochemistry, cell and molecular biology 
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ER  -