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pro vyhledávání: '"J P, Priestle"'
Publikováno v:
Journal of computer-aided molecular design. 13(6)
This paper describes the construction, validation and application of an active site model of the serine protease thrombin. Initial use was made of medium resolution X-ray crystallographic structures of thrombin complexed with low molecular weight, no
Publikováno v:
Advances in experimental medicine and biology. 379
As known from the x-ray crystal structure in complex with a proteinase and from NMR studies, the serine proteinase inhibitor eglin c has a wedge-like shape with a hydrophobic core and a solvent exposed active site binding loop which is stabilized by
Autor:
J P, Priestle
Publikováno v:
Structure (London, England : 1993). 2(10)
Publikováno v:
Journal of molecular biology. 217(2)
The crystal structures of the complexes formed between subtilisin Novo and three inhibitors, eglin c, Arg45-eglin c and Lys53-eglin c have been determined using molecular replacement and difference Fourier techniques and refined at 2.4 A, 2.1 A, and
Autor:
J. P. Priestle
Publikováno v:
Journal of Applied Crystallography. 21:572-576
A suite of Fortran computer programs is described which generates simplified stereo schematic drawings (cartoons) of protein structures similar to the hand-drawn figures of Richardson [Methods Enzymol. (1985), 115, 359–380]. α-helices are represen