Related ArticlesNMR and molecular modeling studies of the interaction between wheat germ agglutinin and the beta-D-GlcpNAc-(1-->6)-alpha-D-Manp epitope present in glycoproteins of tumor cells.
Biochemistry. 2004 Aug 3;43(30):9647-54
Authors: Lycknert K, Edblad M, Imberty A, Widmalm G
The beta-D-GlcpNAc-(1-->6)-alpha-D-Manp disaccharide is a constituent of highly branched cell-surface glycoconjugates that are malignancy markers. The conformational preference of the disaccharide beta-D-GlcpNAc-(1-->6)-alpha-D-Manp-OMe in solution has been studied by molecular modeling and NMR spectroscopy including 1D (1)H,(1)H T-ROESY experiments and analysis of (3)J(H,H) of the hydroxymethyl group being part of the glycosidic linkage of the disaccharide, which revealed the relative populations of the omega torsion angle as gt = 0.60, gg = 0.35, and tg = 0.05. Good agreement was obtained between the effective proton-proton distances from the experiment and those obtained by molecular modeling when the flexibility at the omega torsion angle was taken into account. Molecular modeling of the disaccharide in the binding sites of the lectin wheat germ agglutinin indicates that several conformations could be adopted in the bound state. (1)H NMR and transfer NOESY experiments confirmed that binding took place, and trans-glycosidic proton-proton interactions indicated that a conformational preference was present in the bound state, as observed by the relative change of the NOEs from H1' to H6(pro-R) and H6(pro-S). STD NMR experiments showed that binding occurred in the region of the N-acetyl group of the terminal sugar residue. In addition, the O-methyl group received saturation transfer because of the proximity to the protein. (1)H,(1)H NOEs indicated that the two methyl groups were close in space, as observed in only one of the predicted bound conformations. Experimental and theoretical data therefore agree that one conformation with a gt conformation of the hydroxymethyl group and a negative sign for the psi torsion angle is indeed selected by the lectin upon binding.
[NMR paper] NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
Related Articles NMR and molecular dynamics studies of the interaction of melatonin with calmodulin.
Protein Sci. 2004 Nov;13(11):2925-38
Authors: Turjanski AG, Estrin DA, Rosenstein RE, McCormick JE, Martin SR, Pastore A, Biekofsky RR, Martorana V
Pineal hormone melatonin (N-acetyl-5-methoxytryptamine) is thought to modulate the calcium/calmodulin signaling pathway either by changing intracellular Ca(2+) concentration via activation of its G-protein-coupled...
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[NMR paper] NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-
NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-peptide interactions.
Related Articles NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-peptide interactions.
Carbohydr Res. 2004 Apr 2;339(5):907-28
Authors: Johnson MA, Pinto BM
Investigations of the conformations of carbohydrates, their analogues and their molecular mimics are described, with emphasis on structural and functional information that can be gained by NMR spectroscopic techniques in combination with molecular...
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[NMR paper] Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR.
Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR. II. Roles of nonrepetitive terminal domains and length of repetitive domain.
Related Articles Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR. II. Roles of nonrepetitive terminal domains and length of repetitive domain.
Biopolymers. 2002 Oct 15;65(2):158-68
Authors: Alberti E, Gilbert SM, Tatham AS, Shewry PR, Naito A, Okuda K, Saitô H, Gil AM
This work follows a previous article that addressed the role of disulfide bonds in...
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[NMR paper] Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state
Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state NMR spectroscopy. I. Role of covalent crosslinking.
Related Articles Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state NMR spectroscopy. I. Role of covalent crosslinking.
Biopolymers. 2002;67(6):487-98
Authors: Alberti E, Gilbert SM, Tatham AS, Shewry PR, Gil AM
This work describes a carbon and proton solid-state NMR study of the hydration of a high molecular weight wheat glutenin subunit, 1Dx5. The effect of the presence of...
[NMR paper] 13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a m
13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a magnetically oriented bilayer surface.
Related Articles 13C NMR studies of wheat germ agglutinin interactions with N-acetylglucosamine at a magnetically oriented bilayer surface.
Biochemistry. 1994 Aug 23;33(33):10137-48
Authors: Hare BJ, Rise F, Aubin Y, Prestegard JH
The orientation of synthetic 13C-labeled glycolipid receptors and their interaction with the plant lectin wheat germ agglutinin have been studied in an oriented membrane system using NMR...
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[NMR paper] NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein
NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif Related Articles NMR and molecular modeling studies on two glycopeptides from the carbohydrate-protein linkage region of connective tissue proteoglycans.
Glycobiology. 1999 Jul;9(7):669-77
Authors: Agrawal PK, Jacquinet JC, Krishna NR
Complete 1H and 13C NMR...
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Wheat Germ Cell-Free Protein Production Workshop
Wheat Germ Cell-Free Protein Production Workshop
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The Center for Eukaryotic Structural Genomics (CESG) and the Nuclear Magnetic Resonance Facility at Madison
(NMRFAM) are pleased to announce the first Wheat Germ Cell-Free Protein Production Workshop to be held from
July 30 - August 4, 2006, at the Department of Biochemistry at the University of Wisconsin-Madison in Madison, Wisconsin,
USA. To register for this workshop, complete the Registration Form on the next page and mail in with your NONREFUNDABLE