Related ArticlesNMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion proteins: a loop conformation with histidine and tryptophan in close proximity.
J Biochem. 2000 Aug;128(2):271-81
Authors: Yoshida H, Matsushima N, Kumaki Y, Nakata M, Hikichi K
The N-terminal region of the prion protein from human and mouse contains five tandem repeats with the consensus sequence of PHGGGWGQ. NMR studies were performed in water for two cyclic peptides, cyclo-[C(1)R(2)Q(3)P(4)H(5)G(6)G(7)S(8)W(9)G(10)Q(11)R(12 )D(13)C(14)] (C1) and cyclo-[C(1)R(2)D(3)P(4)H(5)G(6)G(7)G(8)W(9)G(10)Q(11)P(12 )H(13)G(14)G (15)G(16)W(17)G(18)Q(19)R(20)D(21)C(22)] (C2), which are cyclized by a disulfide bridge between the Cys residues at the N- and C-termini, and for their corresponding linear peptides (L1 and L2) which are formed by reduction. The patterns of the C(alpha)H chemical shift difference of these four peptide mimetics were very similar to those observed for the tandem repeats of human prion protein reported by other researchers. The medium-range NOE connectivities were found between the C(beta)H of the H5 and the proton of the W9 side chain for L1. The corresponding NOEs were also observed in H5-W9 and H13-W17 of L2 with ambiguity. These observations indicate that histidine (i) is in close proximity to tryptophan (i+4). d(alphaN) (i,i+2) NOE connectivities were observed between W9 and Q11 of L1 and L2, and d(NN) (i,i+1) NOE connectivities were also observed for G10-Q11 of L1 and L2 and for G18-Q19 of L2. Significantly lower temperature coefficients of amide proton chemical shifts were obtained for Q11 and Q19 of L2 and C2. Structure calculations for L1 showed that HGG(G/S)W and (G/S)WGQ adopt a loop conformation and a beta-turn, respectively. These results strongly suggest that the tandem repeats within prion protein adopt a non-random structure.
[NMR paper] NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II.
NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II.
Related Articles NMR structures of anti-HIV D-peptides derived from the N-terminus of viral chemokine vMIP-II.
Biochem Biophys Res Commun. 2005 Sep 30;335(3):651-8
Authors: Mori M, Liu D, Kumar S, Huang Z
The viral macrophage inflammatory protein-II (vMIP-II) encoded by Kaposi's sarcoma-associated herpesvirus has unique biological activities in that it blocks the cell entry by several different human immunodeficiency virus type 1 (HIV-1) strains via...
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12-01-2010 06:56 PM
[NMR paper] Structure of the model peptides of Bombyx mori silk-elastin like protein studied with
Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR.
Related Articles Structure of the model peptides of Bombyx mori silk-elastin like protein studied with solid state NMR.
Biomacromolecules. 2004 May-Jun;5(3):744-50
Authors: Ohgo K, Kurano TL, Kumashiro KK, Asakura T
The peptides (AG)(6)(VPGVG)(AG)(7) and (AG)(5)(VPGVG)(2)(AG)(5) are models for a new type of protein with both composition and properties such as Bombyx mori silk and elastin. In this paper, we report the solid-state NMR results...
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11-24-2010 09:51 PM
[NMR paper] CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in
CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
Related Articles CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
J Biol Chem. 2003 Dec 12;278(50):50175-81
Authors: Ziegler J, Sticht H, Marx UC, Müller W, Rösch P, Schwarzinger S
The conversion of prion helix 1 from an alpha-helical into an extended conformation is generally assumed to be an essential step in the conversion of the cellular isoform...
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NMR Studies on Domain Diffusion and Alignment in Modular GB1 Repeats.
NMR Studies on Domain Diffusion and Alignment in Modular GB1 Repeats.
Related Articles NMR Studies on Domain Diffusion and Alignment in Modular GB1 Repeats.
Biophys J. 2010 Oct 20;99(8):2636-46
Authors: Walsh JD, Meier K, Ishima R, Gronenborn AM
Modular proteins contain individual domains that are often connected by flexible, unstructured linkers. Using a model system based on the GB1 domain, we constructed tandem repeat proteins and investigated the rotational diffusion and long-range angular ordering behavior of individual domains by measuring...
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[NMR paper] Solid-state NMR studies of the prion protein H1 fragment.
Solid-state NMR studies of the prion protein H1 fragment.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solid-state NMR studies of the prion protein H1 fragment.
Protein Sci. 1996 Aug;5(8):1655-61
Authors: Heller J, Kolbert AC, Larsen R, Ernst M, Bekker T, Baldwin M, Prusiner SB, Pines A, Wemmer DE
Conformational...
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[Question from NMRWiki Q&A forum] Please suggest model proteins and peptides for NMR
Please suggest model proteins and peptides for NMR
do you know any model proteins except lysozyme suitable for nmr experiments?
Check if somebody has answered this question on NMRWiki QA forum
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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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08-21-2010 11:12 PM
[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
...
NMR studies of model peptides of PHGGGWGQ repeats within the N-terminus of prion prot
Linear Mode
