| TECHNOLOGY |
The rapid MOTIONS of ENZYME’s AMINO ACID RESIDUES when it’s in its catalytic transition state have been captured for the first time. Researchers used NMR to detect BACKBONE motion in CYCLOPHILIN A & found movement in one residue to be strongly correlated with the catalytic mechanism. Researchers have used NMR relaxation methods to look for motions in 160 amide nitrogens of title enzyme during catalysis. They detected backbone movements in 10. In nine, these motions turned out to be associated with substrate binding & unbinding. But rate analysis showed that movements of one residue, ARGININE-55, correlated strongly with CATALYSIS. Protein motions have been a missing link in RATIONAL DRUG DESIGN, so pharmaceutical companies may be interested in the technique. Rational drug design has mainly been done by rigid-body docking, “but in the past 10 years, it’s been shown that this usually doesn’t work because you have to take into account the mobility of your protein & drug. This is the kind of problem we are trying to attack in the long term with our experiments – to really go beyond static pictures & explore the proteiu as a DYNAMIC object” |
| UPDATE | 02.02 |
| AUTHOR | This data is not available for free |
| LITERATURE REF. | This data is not available for free |
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