Related Articles1H NMR conformational study on N-terminal nonapeptide sequences of HIV-1 Tat protein: a contribution to structure-activity relationships.
J Pept Sci. 1998 Sep;4(6):400-10
Authors: Mrestani-Klaus C, Fengler A, Brandt W, Faust J, Wrenger S, Reinhold D, Ansorge S, Neubert K
On the basis of our recent results, the N-terminal sequence of HIV-1 Tat protein as a natural competitive inhibitor of dipeptidyl peptidase IV (DP IV) is supposed to interact directly with the active site of DP IV hence mediating its immunosuppressive effects via specific DP IV interactions. Of special interest is the finding that amino acid substitutions of the Tat(1-9) peptide (MDPVDPNIE) in position 5 with S-isoleucine and in position 6 with S-leucine led to peptides with strongly reduced inhibitory activity suggesting differences in the solution conformation of the three analogues. Therefore, 1H NMR techniques in conjunction with molecular modelling have been used here to determine the solution structure of Tat(1-9), I5-Tat(1-9) and L6-Tat(1-9) and to examine the influence of amino acid exchanges on structural features of these peptides. The defined structures revealed differences in the conformations what might be the reason for different interactions of these Tat(1-9) analogues with certain amino acids of the active site of DP IV.
Conformational Study of 9-Dehydro-9-Trifluoromethyl Cinchona Alkaloids via 19F NMR Spectroscopy: Emergence of Trifluoromethyl Moiety as a Conformational Stabilizer and a Probe
Conformational Study of 9-Dehydro-9-Trifluoromethyl Cinchona Alkaloids via 19F NMR Spectroscopy: Emergence of Trifluoromethyl Moiety as a Conformational Stabilizer and a Probe
G. K. Surya Prakash, Fang Wang, Chuanfa Ni, Jingguo Shen, Ralf Haiges, Andrei K. Yudin, Thomas Mathew and George A. Olah
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja202373d/aop/images/medium/ja-2011-02373d_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja202373d
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[NMR paper] Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-
Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-541) of HIV-1 by NMR and MD simulations.
Related Articles Conformational study of fragments of envelope proteins (gp120: 254-274 and gp41: 519-541) of HIV-1 by NMR and MD simulations.
J Pept Sci. 2004 Jun;10(6):363-80
Authors: Kanyalkar M, Srivastava S, Saran A, Coutinho E
The envelope proteins, gp 120 and gp41 of HIV-1, play a crucial role in receptor (CD4+ lymphocytes) binding and membrane fusion. The fragment 254-274 of gp120 is conserved in all strains of...
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[NMR paper] NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding
NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.
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Chembiochem. 2003 Sep 5;4(9):870-7
Authors: Dehner A, Furrer J, Richter K, Schuster I, Buchner J, Kessler H
Hsp90 is one of the most abundant chaperone proteins in the cytosol. In an ATP-dependent manner it plays an essential role in the folding and activation of a...
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[NMR paper] The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular
The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular dichroism and (1)H NMR spectroscopy in aqueous and membrane-like environments.
Related Articles The cytoplasmic helix of cannabinoid receptor CB2, a conformational study by circular dichroism and (1)H NMR spectroscopy in aqueous and membrane-like environments.
J Pept Res. 2002 Sep;60(3):169-77
Authors: Choi G, Landin J, Xie XQ
The cytoplasmic helix domain (fourth cytoplasmic loop, helix 8) of numerous G protein-coupled receptors (GPCRs) such as rhodopsin and...
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[NMR paper] Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-ci
Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR.
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FEBS Lett. 1998 Jan 30;422(2):201-4
Authors: Gröbner G, Choi G, Burnett IJ, Glaubitz C, Verdegem PJ, Lugtenburg J, Watts A
Rhodopsin is the retinal photoreceptor responsible for visual signal transduction. To determine the orientation and...
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[NMR paper] Pilin C-terminal peptide binds asialo-GM1 in liposomes: a 2H-NMR study.
Pilin C-terminal peptide binds asialo-GM1 in liposomes: a 2H-NMR study.
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 Pilin C-terminal peptide binds asialo-GM1 in liposomes: a 2H-NMR study.
Protein Sci. 1997 Nov;6(11):2459-61
Authors: Jones DH, Hodges RS, Barber KR, Grant CW
Wideline 2H-NMR observations are...
[NMR paper] 31P-NMR assignment and conformational study of NADPH bound to Lactobacillus casei dih
31P-NMR assignment and conformational study of NADPH bound to Lactobacillus casei dihydrofolate reductase based on two-dimensional 1H-31P-heteronuclear and 1H-detected 1H-31P-shift-correlation experiments.
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 31P-NMR assignment and conformational study of NADPH bound to Lactobacillus casei dihydrofolate reductase based on two-dimensional 1H-31P-heteronuclear and 1H-detected 1H-31P-shift-correlation experiments.
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