Robust Identification of Binding Hot Spots Using Continuum Electrostatics: Application to Hen Egg-White Lysozyme
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چکیده
منابع مشابه
Robust Identification of Binding Hot Spots Using Continuum Electrostatics: Application to Hen Egg-White Lysozyme
Binding hot spots, protein regions with high binding affinity, can be identified by using X-ray crystallography or NMR spectroscopy to screen libraries of small organic molecules that tend to cluster at such hot spots. FTMap, a direct computational analogue of the experimental screening approaches, uses 16 different probe molecules for global sampling of the surface of a target protein on a den...
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Proton tautomerism is a general phenomenon in organic molecules and plays a vital role in many fields of chemistry and biochemistry. The tautomerism of salicylideneanilines [eq(1)] has attracted a considerable attention because it is closely related to thermoand photochromism. Salicylideneanilines greatly favor the enol form over the cis-keto form in the gas phase. We demonstrate here that the ...
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The present studies were carried out essentially as described by Moult et al. [3]. Tetragonal crystals of hen egg-white lysozyme [4] were grown at pH 4.7 in 0.02 M acetate buffer, containing 5% NaCl (w/v). Individual crystals (space group P4s2r2, a=b=79.1 A, C= 37.9 A) about 0.6 mm in the longest dimension, were transferred to 1 .O mm diameter quartz capillaries containing 0.1 ml mother liquor....
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Divalent copper was found to inhibit non-competitively the lysis of Micrococcus lysodeikticus cells by hen egg-white lysozyme, with an inhibition constant K, = 3.8 X lo2 M-l. The association constants of Cu2+ for lysozyme and for a derivative of lysozyme in which tryptophan residue 108 was selectively modified, were measured spectrofluorimetrically and found to be 1.8 X lo2 M-l and 1.0 X lo3 M-...
متن کاملCharacterization of the unfolding pathway of hen egg white lysozyme.
After the recent discovery of a ribonuclease A unfolding intermediate [Kiefhaber, T., et al. (1995) Nature 375, 513-515], we investigated the unfolding pathway of hen egg white lysozyme. At pH* 4.00 with D2O at 10 degrees C and 6 M guanidinium chloride, unfolding shows a single, slow kinetic phase, with a relaxation time of 3300 s when monitored by circular dichroism (CD). Exchange of the trypt...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2011
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja207914y