Related ArticlesNMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
Biochemistry. 2002 Feb 19;41(7):2149-57
Authors: Johnson MA, Rotondo A, Pinto BM
Transferred nuclear Overhauser enhancement (TRNOE) experiments have been performed at 800 MHz to investigate the bound conformation of the hexapeptide DRPVPY, a functional molecular mimic of the group A Streptococcus cell-wall polysaccharide. The hexapeptide binds to the monoclonal antibody SA-3, mimicking the branched trisaccharide repeating unit, L-Rha-alpha-(1 --> 2)-(D-GlcNAc-beta-(1 --> 3))-alpha-L-Rha (Rha, rhamnose; GlcNAc, N-acetylglucosamine). The peptide adopts a tight turn conformation with close contacts between the side chains of valine and tyrosine. Relaxation network editing experiments (QUIET-NOESY) were used to confirm the validity of the observed contacts and to evaluate the presence of spin diffusion pathways. Saturation transfer difference (STD-NMR) experiments with selective saturation of protein resonances revealed enhancements of many of the peptide resonances due to close contacts between the peptide and the protein within the antibody combining site.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
FEBS Lett. 2011 Apr 20;585(8):1197-202
Authors: Moehle K, Freund A, Kubli E, Robinson JA
The insect sex peptide (SP) elicits a variety of biological responses upon transfer to the mated female. SP contains 36 amino acids, including a tryptophan-rich N-terminal region, a central region containing five hydroxyproline (Hyp) residues, and a C-terminal region enclosed by a...
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Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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02-08-2011 06:28 PM
[NMR paper] Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular d
Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study.
Related Articles Micelle-bound conformation of a hairpin-forming peptide: combined NMR and molecular dynamics study.
Biopolymers. 2002 Nov 15;65(4):284-98
Authors: Dixon AM, Venable RM, Pastor RW, Bull TE
A peptide fragment from a protein hairpin turn region was modified by addition of isoleucine residues to both ends to enhance binding to lipid micelles; the resulting peptide (I(1)-I(2)-C(3)-N(4)-N(5)-P(6)-H(7)-I(8)-I(9)) contains the core...
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11-24-2010 08:58 PM
[NMR paper] NMR studies on the conformation of the CD4 36-59 peptide bound to HIV-1 gp120.
NMR studies on the conformation of the CD4 36-59 peptide bound to HIV-1 gp120.
Related Articles NMR studies on the conformation of the CD4 36-59 peptide bound to HIV-1 gp120.
Biochemistry. 1998 Jul 28;37(30):10616-25
Authors: Gizachew D, Moffett DB, Busse SC, Westler WM, Dratz EA, Teintze M
A peptide containing residues 36-59 of the human CD4 receptor includes most of the residues thought to be involved in binding the HIV surface glycoprotein, gp120. This peptide was synthesized and inhibited the binding of gp120 to soluble CD4. NMR relaxation...
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11-17-2010 11:15 PM
[NMR paper] NMR and CD studies on the conformation of a synthetic peptide containing epitopes of
NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41.
Related Articles NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41.
Biopolymers. 1996 Mar;38(3):423-35
Authors: Consonni R, Limiroli R, Longhi R, Manera E, Vecchio G, Ragona L, Siccardi AG, Zetta L
CD and nmr characterizations are reported for the 23-mer peptide CMC3, corresponding to residues 577-599...
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08-22-2010 02:27 PM
[NMR paper] NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and port
NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Related Articles NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Biochemistry. 1991 Jul 2;30(26):6574-83
Authors: Fesik SW, Gampe RT, Eaton HL, Gemmecker G, Olejniczak ET, Neri P, Holzman TF, Egan DA, Edalji R, Simmer R
Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with...
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08-21-2010 11:12 PM
[NMR paper] NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and port
NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Related Articles NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Biochemistry. 1991 Jul 2;30(26):6574-83
Authors: Fesik SW, Gampe RT, Eaton HL, Gemmecker G, Olejniczak ET, Neri P, Holzman TF, Egan DA, Edalji R, Simmer R
Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with...
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08-21-2010 11:12 PM
[NMR paper] Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV
Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nsb.gif Related Articles Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.
Nat Struct Biol. 1999 Feb;6(2):141-5
Authors: Weliky DP, Bennett AE, Zvi A, Anglister J, Steinbach PJ, Tycko R
Solid-state NMR measurements have been carried out on frozen solutions of the complex of a 24-residue peptide derived from the third variable...
NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
Linear Mode
