Related ArticlesOne- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.
J Protein Chem. 1990 Apr;9(2):129-36
Authors: Dill K, Hu SH, Berman E, Pavia AA, Lacombe JM
One- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy (at 11.7 Tesla) was used to gain some structural and spectral information about glycophorin AM, glycophorin AM tryptic glycopeptide, a related pentapeptide, and two related monoglycosylated pentapeptides. The protein spectral information suggests that the highly glycosylated N-terminus of glycophorin does not seem to possess a unique tertiary structure. Furthermore, the spectral information provided by the carbohydrate residues also indicates that there is no strong carbohydrate-protein interaction resulting in a unique tertiary structure. This result does not preclude any unique protein-carbohydrate interactions. For the small monoglycosylated pentapeptide containing alpha-D-GalNAc attached to Thr, a unique NOESY cross-peak was observed between the anomeric proton and the beta-proton of Thr. A cross-peak between the beta-proton of Ser and the anomeric proton was not observed for a related monoglycosylated pentapeptide containing alpha-D-GalNAc O-linked to Ser.
[NMR paper] Interaction between an amantadine analogue and the transmembrane portion of the influ
Interaction between an amantadine analogue and the transmembrane portion of the influenza A M2 protein in liposomes probed by 1H NMR spectroscopy of the ligand.
Related Articles Interaction between an amantadine analogue and the transmembrane portion of the influenza A M2 protein in liposomes probed by 1H NMR spectroscopy of the ligand.
J Med Chem. 2004 Sep 23;47(20):4975-8
Authors: Kolocouris A, Hansen RK, Broadhurst RW
1H NMR spectroscopy of a fluoroamantadine ligand was used to probe the pH dependence of binding to the transmembrane peptide...
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[NMR paper] Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as
Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective 13C labeling of the glycans.
Related Articles Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective 13C labeling of the glycans.
J Biomol NMR. 1998 Oct;12(3):385-94
Authors: Yamaguchi Y, Kato K, Shindo M, Aoki S, Furusho K, Koga K, Takahashi N, Arata Y, Shimada I
A systematic method for 13C labeling of the glycan of...
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[NMR paper] 1H NMR studies of the effects of glycosylation on the C-terminal pentapeptide of pept
1H NMR studies of the effects of glycosylation on the C-terminal pentapeptide of peptide T.
Related Articles 1H NMR studies of the effects of glycosylation on the C-terminal pentapeptide of peptide T.
Biomed Pept Proteins Nucleic Acids. 1996;2(2):59-66
Authors: Wilce JA, Otvos L, Craik DJ
The C-terminal pentapeptide of peptide T (T5) and a glycosylated analogue (T5GlcNAc) were investigated using 1H NMR spectroscopy to examine the influence of the sugar on the secondary structural characteristics of the peptide. The NMR data confirm the...
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[NMR paper] 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal ta
1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
Related Articles 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1.
Biochemistry. 1994 Mar 15;33(10):2838-42
Authors: Lycksell PO, Ingemarson R, Davis R, Gräslund A, Thelander L
Mouse ribonucleotide reductase...
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[NMR paper] NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A pro
NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR studies of U1 snRNA recognition by the N-terminal RNP domain of the human U1A protein.
EMBO J. 1994 Aug 15;13(16):3873-81
Authors: Howe PW, Nagai K, Neuhaus D, Varani G
The RNP domain is a very common motif found in hundreds of proteins, including many protein components of the RNA processing machinery. The 70-90...
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[NMR paper] 2H-NMR investigation of DMPC/glycophorin bilayers.
2H-NMR investigation of DMPC/glycophorin bilayers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 2H-NMR investigation of DMPC/glycophorin bilayers.
Biochim Biophys Acta. 1994 Jul 13;1193(1):127-37
Authors: Shan X, Davis JH, Chu JW, Sharom FJ
Deuterium nuclear magnetic resonance spectroscopy was used to investigate the phase equilibria, and the temperature and concentration dependences of the phospholipid hydrocarbon chain order, of mixtures of glycophorin in...
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[NMR paper] 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependen
1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: a leucine/isoleucine zipper.
Related Articles 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: a leucine/isoleucine zipper.
Biochemistry. 1991 Oct 1;30(39):9387-95
Authors: Atkinson RA, Saudek V, Huggins JP, Pelton JT
Cyclic GMP dependent protein kinase exists as a dimer in its native form. A peptide corresponding to the dimerization domain in the N-terminal segment has been characterized...
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[NMR paper] 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependen
1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: a leucine/isoleucine zipper.
Related Articles 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: a leucine/isoleucine zipper.
Biochemistry. 1991 Oct 1;30(39):9387-95
Authors: Atkinson RA, Saudek V, Huggins JP, Pelton JT
Cyclic GMP dependent protein kinase exists as a dimer in its native form. A peptide corresponding to the dimerization domain in the N-terminal segment has been characterized...