Zobrazeno 1 - 10
of 34
pro vyhledávání: '"F. L. SUDDATH"'
Autor:
James C. Powers, Edward M. Burgess, John E. Kerrigan, R. Richard Plaskon, F. L. Suddath, Chih-Min Kam
Publikováno v:
Archives of Biochemistry and Biophysics. 300:588-597
Kinetic measurements for the inhibition of porcine pancreatic elastase by 7-substituted 4-chloro-.3-ethox-yisocoumarins were performed. To obtain possible explanations for the kinetic results, structures resulting from energy minimizations of inhibit
Publikováno v:
Biophysical journal. 37(1)
Autor:
R. Richard Plaskon, Chih-Min Kam, John E. Kerrigan, Edward J. Duffy, James C. Powers, Pete Lollar, F. L. Suddath
Publikováno v:
Journal of medicinal chemistry. 37(9)
A series of 7-amino-4-chloro-3-(3-isothioureidopropoxy)isocoumarin (NH2-CiTPrOIC) derivatives with various substituents at the 7- and 3-positions have been synthesized as inhibitors of several blood coagulation enzymes. Isocoumarins substituted with
Publikováno v:
Proteins. 13(2)
A step leading to the formation of the covalent complexes between porcine pancreatic elastase (PPE) and 7-[(alkylcarbamoyl)amino]-4-chloro-3-ethoxyisocoumarins (alkylHNCO-EICs) is the formation of the noncovalent Michaelis complex. No average structu
Autor:
F. L. Suddath, Trevor J. Greenhough
Publikováno v:
Journal of Applied Crystallography. 19:400-409
The accuracy of oscillation camera data in macromolecular crystallography is dependent upon a variety of factors including crystal quality, experimental conditions and the processing of the data itself. In cases where the best possible data have been
Publikováno v:
Nucleic Acids Research. 2:2329-2342
The atomic coordinates of yeast phenylalanine transfer RNA (tRNA) as well as the torsion angles of the polynucleotide chain are presented as derived from an x-ray diffraction analysis of orthorhombic crystals. A comparison is made between the coordin
Publikováno v:
Journal of Biological Chemistry. 257:13278-13282
The three-dimensional crystal structure of the mitogenic lectin from the green pea (Pisum sativum) has been determined at 6-A resolution by x-ray diffraction methods. Pea lectin was isolated by use of affinity chromatography and was crystallized from