Related ArticlesSolution 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 conformation has been predicted for this highly positively charged N-terminal region [Argos, P. (1981) Virology 110, 55-62; Vriend, G., Verduin, B. J. M., & Hemminga, M. A. (1986) J. Mol. Biol. 191, 453-460], no experimental evidence for this conformation has been presented so far. In this study, two-dimensional proton NMR experiments were performed on a chemically synthesized pentacosapeptide containing the first 25 amino acids of this coat protein [Ten Kortenaar, P. B. W., Krüse, J., Hemminga, M. A., & Tesser, G. I. (1986) Int. J. Pept. Protein Res. 27, 401-413]. All resonances could be assigned by a combined use of two-dimensional correlated spectroscopy and nuclear Overhauser enhancement spectroscopy carried out at four different temperatures. Various NMR parameters indicate the presence of a conformational ensemble consisting of helical structures rapidly converting into more extended states. Differences in chemical shifts and nuclear Overhauser effects indicate that lowering the temperature induces a shift of the dynamic equilibrium toward more helical structures. At 10 degrees C, a perceptible fraction of the conformational ensemble consists of structures with an alpha-helical conformation between residues 9 and 17, likely starting with a turnlike structure around Thr9 and Arg10. Both the conformation and the position of this helical region agree well with the secondary structure predictions mentioned above.
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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[NMR paper] NMR structure and peptide hormone binding site of the first extracellular domain of a
NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.
Related Articles NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.
Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12836-41
Authors: Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R
The corticotropin-releasing factor (CRF) ligand family has diverse effects on the CNS, including the modulation of the stress response. The ligands'...
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[NMR paper] NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein
NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Related Articles NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Biochemistry. 2004 Feb 24;43(7):1854-61
Authors: Rosal R, Pincus MR, Brandt-Rauf PW, Fine RL, Michl J, Wang H
We have recently found that a peptide from the mdm-2 binding domain of the p53 protein induced rapid membranolytic necrosis of a variety of different human...
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11-24-2010 09:25 PM
[NMR paper] NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.
NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.
Related Articles NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.
J Mol Biol. 1999 Sep 10;292(1):181-90
Authors: Kobayashi N, Freund SM, Chatellier J, Zahn R, Fersht AR
A detailed structural analysis of interactions between denatured proteins and GroEL is essential for an understanding of its mechanism. Minichaperones constitute an excellent paradigm for obtaining high-resolution structural information about the binding site and...
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11-18-2010 08:31 PM
[NMR paper] NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+
NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
Related Articles NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
Biochemistry. 1999 Sep 21;38(38):12320-32
Authors: Elshorst B, Hennig M, Försterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E
The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the...
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[NMR paper] Determination of the solution structure of a synthetic two-site calcium-binding homod
Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
Related Articles Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
Biochemistry. 1992 Oct 13;31(40):9572-80
Authors: Shaw GS, Hodges RS, Sykes BD
The solution structure of a 34-residue synthetic calcium-binding peptide from site III of chicken troponin-C has been determined by 1H NMR spectroscopy. In solution and in the presence of calcium...
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[NMR paper] Conformational studies on a peptide fragment representing the RNA-binding N-terminus
Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
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 Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
Eur J Biochem. 1991 Oct 15;201(2):489-94
Authors: van der Graaf M, Hemminga MA
...
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[NMR paper] Conformational studies on a peptide fragment representing the RNA-binding N-terminus
Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
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 Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy.
Eur J Biochem. 1991 Oct 15;201(2):489-94
Authors: van der Graaf M, Hemminga MA
...