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 disulfide bridge. The solution structure of SP, studied here using NMR spectroscopy, includes a motif WPWN that adopts a type I ?-turn in the N-terminal Trp-rich region. This turn region is connected to the central Hyp-rich region, which adopts extended and/or PPII-like conformations. The C-terminal disulfide-bonded loop populates helical turns or nascent helical structure. Overall, the results reveal a rather flexible peptide that lacks a compact folded structure in solution.
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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[NMR paper] NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
NMR studies of the antibody-bound conformation of a carbohydrate-mimetic peptide.
Related Articles NMR 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...
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11-24-2010 08:49 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] The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of
The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of the folding of a synthetic model for the DNA-binding loop of the ssDNA-binding protein encoded by gene V of phage M13.
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 The solution structure of the synthetic circular peptide CGVSRQGKPYC. NMR studies of the folding of a synthetic model for the DNA-binding loop of the ssDNA-binding protein encoded by gene V of phage M13.
Eur...
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[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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[NMR paper] NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reve
NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.
EMBO J. 1995 Jul 17;14(14):3563-71
Authors: Bycroft M, Grünert S, Murzin AG, Proctor M, St Johnston D
The...
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[NMR paper] Solution conformation of a peptide fragment representing a proposed RNA-binding site
Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMR.
Related Articles Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMR.
Biochemistry. 1991 Jun 11;30(23):5722-7
Authors: van der Graaf M, van Mierlo CP, Hemminga MA
The first 25 amino acids of the coat protein of cowpea chlorotic mottle virus are essential for binding the encapsidated RNA. Although an alpha-helical...
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08-21-2010 11:16 PM
Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts
Abstract We present a program, named Promega, to predict the Xaa-Pro peptide bond conformation on the basis of backbone chemical shifts and the amino acid sequence. Using a chemical shift database of proteins of known structure together with the PDB-extracted amino acid preference of cis Xaa-Pro peptide bonds, a cis/trans probability score is calculated from the backbone and 13Cβ chemical shifts of the proline and its neighboring residues. For an arbitrary number of input chemical shifts, which may include Pro-13Cγ, Promega calculates the statistical probability that a Xaa-Pro peptide bond...
NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.
Linear Mode
