The Biochemical journal, 308 ( Pt 1), 251-260 (1995-05-15)
Tryptophan and 5-bromotryptophan (5-BrTrp) are relatively potent inhibitors of sickle-haemoglobin polymerization. The binding sites of these compounds to normal and sickle haemoglobin (HBA and HBS) have been suggested, but not firmly established, through the use of spin-labelled derivatives and/or computer
Journal of molecular biology, 244(1), 1-5 (1994-11-18)
The trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis has been crystallized and examined by crystallography using X-ray synchrotron radiation diffraction data. Crystals of TRAP complexed with L-tryptophan belong to space group C2 with a = 156.8 A, b =
Journal of medicinal chemistry, 33(12), 3138-3142 (1990-12-01)
5-Bromotryptophan (5-BrTrp) is the most potent amino acid derivative reported in the literature to inhibit the gelation of hemoglobin S (from sickle cell anemia patients). Trp-Trp is also more potent than Trp as an antigelation agent. Therefore, we have prepared
Journal of molecular biology, 223(3), 791-800 (1992-02-05)
The binding sites of indole-based gelation inhibitors with sickle cell hemoglobin were investigated by two parallel theoretical approaches. A geometric approach originated by Kuntz and co-workers uses a spatial buildup scheme to locate potential binding regions, while a hybrid grid/geometric
Protein modifications are often detected by precursor ion scanning. When quadrupole TOF mass spectrometers are used for precursor ion scanning with high-resolution, high-accuracy fragment ion selection, "reporter" ions are required to have a unique mass within +/-0.04 Da or less
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