[NMR paper] NMR-based determination of the binding epitope and conformational analysis of MUC-1 g
NMR-based determination of the binding epitope and conformational analysis of MUC-1 glycopeptides and peptides bound to the breast cancer-selective monoclonal antibody SM3.
Related Articles NMR-based determination of the binding epitope and conformational analysis of MUC-1 glycopeptides and peptides bound to the breast cancer-selective monoclonal antibody SM3.
Eur J Biochem. 2002 Mar;269(5):1444-55
Authors: Möller H, Serttas N, Paulsen H, Burchell JM, Taylor-Papadimitriou J,
Mucin glycoproteins on breast cancer cells carry shortened...
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11-24-2010 08:49 PM
[NMR paper] 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides.
1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides.
Related Articles 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides.
J Biol Chem. 2001 Jul 6;276(27):25150-6
Authors: Wintjens R, Wieruszeski JM, Drobecq H, Rousselot-Pailley P, Buée L, Lippens G, Landrieu I
The recent crystal structure of Pin1 protein bound to a doubly phosphorylated peptide from the C-terminal domain of RNA polymerase II revealed that binding interactions between Pin1 and its substrate take place through its...
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11-19-2010 08:32 PM
[NMR paper] NMR studies of peptides derived from the putative binding regions of cartilage protei
NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
Related Articles NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
J Biol Chem. 1994 Jan 21;269(3):1699-704
Authors: Horita DA, Hajduk PJ, Goetinck PF, Lerner LE
Previous work has implicated sequences within the tandem repeats of cartilage link protein in the interaction of link protein with hyaluronan. This conclusion was based on...
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08-22-2010 03:33 AM
[NMR paper] NMR studies of peptides derived from the putative binding regions of cartilage protei
NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
Related Articles NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
J Biol Chem. 1994 Jan 21;269(3):1699-704
Authors: Horita DA, Hajduk PJ, Goetinck PF, Lerner LE
Previous work has implicated sequences within the tandem repeats of cartilage link protein in the interaction of link protein with hyaluronan. This conclusion was based on...
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08-22-2010 03:33 AM
[NMR paper] The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli pho
The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system.
FEBS Lett. 1993 Jan 2;315(1):11-5
Authors: van Nuland NA, Kroon GJ, Dijkstra K, Wolters GK, Scheek RM, Robillard GT
The region of the surface of...
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08-21-2010 11:53 PM
[NMR paper] Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Related Articles Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Biochemistry. 1991 Jun 4;30(22):5524-31
Authors: Gehring K, Williams PG, Pelton JG, Morimoto H, Wemmer DE
Tritium-labeled alpha- and beta-maltodextrins have been used to study their complexes with maltose-binding protein (MBP), a 40-kDa bacterial protein. Five substrates, from maltose to maltohexaose, were labeled at their reducing ends and their binding studied. Tritium NMR spectroscopy...
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08-21-2010 11:16 PM
[NMR paper] Direct measurement of agonist binding to genetically engineered peptides of the acety
Direct measurement of agonist binding to genetically engineered peptides of the acetylcholine receptor by selective T1 NMR relaxation.
Related Articles Direct measurement of agonist binding to genetically engineered peptides of the acetylcholine receptor by selective T1 NMR relaxation.
Biochemistry. 1990 Mar 13;29(10):2617-22
Authors: Fraenkel Y, Navon G, Aronheim A, Gershoni JM
Interactions of four ligands of the nicotinic acetylcholine receptor with genetically engineered peptides have been studied by NMR. A recombinant cholinergic binding...
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08-21-2010 10:48 PM
Precise structural determination of weakly binding peptides by utilizing dihedral ang
Abstract Structural determination of target-bound conformations of peptides is of primary importance for the optimization of peptide ligands and peptideâ??mimetic design. In the structural determination of weakly binding ligands, transferred nuclear Overhauser effect (TrNOE) methods have been widely used. However, not many distance constraints can be obtained from small peptide ligands by TrNOE, especially for peptides bound to a target molecule in an extended conformation. Therefore, for precise structural determination of weakly binding peptides, additional structural constraints are...
Isolation of ZnO-Binding 12-mer Peptides and Determination of Their Binding Epitopes by NMR Spectroscopy
Linear Mode
