Two pyrenylalanines in dihydrofolate reductase form an excimer enabling the study of protein dynamics.
Two pyrenylalanines in dihydrofolate reductase form an excimer enabling the study of protein dynamics.
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DOI：
10.1021/ja307179q
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发表时间：
2012-11-21
影响因子：
15
通讯作者：
Hecht SM
中科院分区：
文献类型：
--
作者：
Chen S;Wang L;Fahmi NE;Benkovic SJ;Hecht SM
Because of the lack of sensitivity to small changes in distance by available FRET pairs (a constraint imposed by the dimensions of the enzyme), a DHFR containing two pyrene moieties was prepared to enable the observation of excimer formation. Pyren-1-ylalanine was introduced into DHFR positions 16 and 49 using an in vitro expression system in the presence of pyren-1-ylalanyl-tRNACUA. Excimer formation (λex 342 nm; λem 481 nm) was observed in the modified DHFR, which retained its catalytic competence and was studied under multiple and single turnover conditions. The excimer appeared to follow a protein conformational change after the H transfer involving the relative position and orientation of the pyrene moieties and is likely associated with product dissociation.
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影响因子：
14.9
作者：
ROBERTSON, SA;NOREN, CJ;SCHULTZ, PG
通讯作者：
SCHULTZ, PG
影响因子：
56.9
作者：
NOREN, CJ;ANTHONYCAHILL, SJ;SCHULTZ, PG
通讯作者：
SCHULTZ, PG
影响因子：
--
作者：
Belokon', YN;Tararov, VI;Ryzhov, MG
通讯作者：
Ryzhov, MG
影响因子：
48
作者：
Ryu, YH;Schultz, PG
通讯作者：
Schultz, PG
影响因子：
2.1
作者：
HECKLER, TG;CHANG, LH;HECHT, SM
通讯作者：
HECHT, SM