Related ArticlesSequential 1H NMR assignments of kistrin, a potent platelet aggregation inhibitor and glycoprotein IIb-IIIa antagonist.
Biochemistry. 1992 Feb 4;31(4):1031-9
Authors: Adler M, Wagner G
Sequence-specific nuclear magnetic resonances assignments have been obtained for the protons of kistrin. Kistrin is a small naturally occurring snake venom protein that inhibits platelet aggregation by blocking the interaction of fibrinogen with the membrane-bound glycoprotein IIb-IIIa (GP IIb-IIIa), a receptor from the integrin family. Kistrin has an Arg-Gly-Asp sequence which is believed to form an adhesion recognition sequence that is essential for activity. Therefore, the interaction between kistrin and GP IIb-IIIa may provide important information on the motif used by integrins to recognize their target proteins which bear RGD sequences. Kistrin consists of 68 residues and contains six intramolecular disulfide bonds. Although one-third of the amide protons are protected from exchange with the solvent, there appears to be little or no regular secondary structure. The large number of NOE's between residues separated by two and three positions in the sequence indicates that the protein contains a large number of tightly packed loops. Along with the sequential assignments, this paper also discusses the construction and use of computerized data bases for manipulating NMR results. A strategy for computer-assisted sequential resonance using these data bases is also presented.
Solid-state NMR sequential assignments of ?-synuclein.
Solid-state NMR sequential assignments of ?-synuclein.
Solid-state NMR sequential assignments of ?-synuclein.
Biomol NMR Assign. 2011 Jul 9;
Authors: Gath J, Habenstein B, Bousset L, Melki R, Meier BH, Böckmann A
Parkinson's disease is amongst the most frequent and most devastating neurodegenerative diseases. It is tightly associated with the assembly of proteins into high-molecular weight protein species, which propagate between neurons in the central nervous system. The principal protein involved in this process is ?-synuclein which is a...
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[NMR paper] The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061--fr
The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061--from the NMR tube to the clinic.
Related Articles The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061--from the NMR tube to the clinic.
Biopolymers. 2004;76(4):309-23
Authors: Tsantrizos YS
The virally encoded serine protease NS3/NS4A is essential to the life cycle of the hepatitis C virus (HCV), an important human pathogen causing chronic hepatitis, cirrhosis of the liver, and hepatocellular carcinoma. Until very recently, the...
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Discovery of a potent and selective Bcl-2 inhibitor using SAR by NMR.
Discovery of a potent and selective Bcl-2 inhibitor using SAR by NMR.
Related Articles Discovery of a potent and selective Bcl-2 inhibitor using SAR by NMR.
Bioorg Med Chem Lett. 2010 Sep 15;
Authors: Petros AM, Huth JR, Oost T, Park CM, Ding H, Wang X, Zhang H, Nimmer P, Mendoza R, Sun C, Mack J, Walter K, Dorwin S, Gramling E, Ladror U, Rosenberg SH, Elmore SW, Fesik SW, Hajduk PJ
The Bcl-2 family of proteins plays a major role in the regulation of apoptosis, or programmed cell death. Overexpression of the anti-apoptotic members of this...
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[NMR paper] Sequential 1H, 13C, and 15N NMR assignments and solution conformation of apokedarcidi
Sequential 1H, 13C, and 15N NMR assignments and solution conformation of apokedarcidin.
Related Articles Sequential 1H, 13C, and 15N NMR assignments and solution conformation of apokedarcidin.
Biochemistry. 1994 Sep 27;33(38):11438-52
Authors: Constantine KL, Colson KL, Wittekind M, Friedrichs MS, Zein N, Tuttle J, Langley DR, Leet JE, Schroeder DR, Lam KS
Kedarcidin is a recently discovered antitumor antibiotic chromoprotein. The solution conformation of the kedarcidin apoprotein (114 residues) has been characterized by heteronuclear...
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[NMR paper] Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and sec
Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution.
Related Articles Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution.
Biochemistry. 1991 Jun 25;30(25):6330-41
Authors: Carr MD, Birdsall B, Frenkiel TA, Bauer CJ, Jimenez-Barbero J, Polshakov VI, McCormick JE, Roberts GC, Feeney J
Three-dimensional (3D) heteronuclear NMR techniques have been used to make sequential 1H and 15N resonance...
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[NMR paper] 1H-NMR studies of bovine platelet factor 4: histidine assignments and interactions wi
1H-NMR studies of bovine platelet factor 4: histidine assignments and interactions with heparin.
Related Articles 1H-NMR studies of bovine platelet factor 4: histidine assignments and interactions with heparin.
Biochim Biophys Acta. 1991 Jun 24;1078(2):208-18
Authors: Talpas CJ, Walz DA, Lee L
1H-NMR spectroscopy has been used to assign and to characterize the two histidine C2H resonances of the heparin binding protein, bovine platelet factor 4. One histidine has a pKa value of 6.51 at 27 degrees C; the second histidine exhibits 2 pKa values...
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[NMR paper] 1H NMR studies of echistatin in solution. Sequential resonance assignments and second
1H NMR studies of echistatin in solution. Sequential resonance assignments and secondary structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H NMR studies of echistatin in solution. Sequential resonance assignments and secondary structure.
Eur J Biochem. 1991 Dec 5;202(2):315-21
Authors: Dalvit C, Widmer H, Bovermann G, Breckenridge R, Metternich R
Two-dimensional 1H-NMR methods have been used to obtain complete proton...
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[NMR paper] Sequential 1H NMR assignments and secondary structure of the B domain of staphylococc
Sequential 1H NMR assignments and secondary structure of the B domain of staphylococcal protein A: structural changes between the free B domain in solution and the Fc-bound B domain in crystal.
Related Articles Sequential 1H NMR assignments and secondary structure of the B domain of staphylococcal protein A: structural changes between the free B domain in solution and the Fc-bound B domain in crystal.
Biochemistry. 1990 Sep 18;29(37):8787-93
Authors: Torigoe H, Shimada I, Saito A, Sato M, Arata Y
The recombinant B domain (FB) of staphylococcal...