Related ArticlesConformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
Biochemistry. 1997 Apr 22;36(16):5045-52
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational changes between the GMPPNP form of human N-ras P21 as compared to GDP and GTPgammaS forms. Full-length N-ras P21 was also compared with protein truncated beyond residue 167, to search for interaction points between the more invariant part of the protein and the variable C-terminal section. In both cases, the reporter was the 15N-H 2D spectrum of aspartate amide groups labeled with 15N. Small truncation-induced changes were seen in the spectrum at the resonances of Asp-54, -108, and -109 which are not far from the C-terminal and, surprisingly, at Asp-57 which is more remote. The spectrum obtained for the GMPPNP-ligated form is similar to that of the GTPgammaS form, except that peaks of several residues are weak at low temperature, and strongly temperature-dependent in their intensity, and a new resonance appears at 15 degrees C and above. The observations are discussed in terms of a two-state model for the GMPPNP-ligated protein, previously proposed by Geyer et al. [(1996) Biochemistry 35, 10308-10320].
Neurotoxin II Bound to Acetylcholine Receptors in Native Membranes Studied by Dynamic Nuclear Polarization NMR
Neurotoxin II Bound to Acetylcholine Receptors in Native Membranes Studied by Dynamic Nuclear Polarization NMR
Arne H. Linden, Sascha Lange, W. Trent Franks, U?mit Akbey, Edgar Specker, Barth-Jan van Rossum and Hartmut Oschkinat
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206999c/aop/images/medium/ja-2011-06999c_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206999c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/4d1LYPHtCFw
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[NMR paper] NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the
NMR conformational studies of micelle-bound orexin-B: a neuropeptide involved in the sleep/awake cycle and feeding regulation.
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J Biomol Struct Dyn. 2003 Dec;21(3):341-51
Authors: Miskolzie M, Lucyk S, Kotovych G
The preferred conformation of orexin-B, an orphan G-protein coupled receptor agonist (the human sequence is RSGPPGLQGRLQRLLQASGNHAAGILTM-NH(2)) has been determined by (1)H and (13)C 2D NMR...
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[NMR paper] Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GM
Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR.
Biochemistry. 1997 Apr 22;36(16):5045-52
Authors: Hu JS, Redfield AG
Heteronuclear-edited proton-detected NMR methods are used to study the nucleotide-dependent conformational changes between the GMPPNP form of human N-ras P21...
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08-22-2010 03:31 PM
[NMR paper] Conformational differences of ovine and human corticotropin releasing hormone. A CD,
Conformational differences of ovine and human corticotropin releasing hormone. A CD, IR, NMR and dynamic light scattering study.
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Int J Pept Protein Res. 1996 May;47(5):383-93
Authors: Dathe M, Fabian H, Gast K, Zirwer D, Winter R, Beyermann M, Schümann M, Bienert M
The differences in the conformational properties of ovine (o) and human (h) CRH in aqueous solution, structure-inducing TFE and in the...
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[NMR paper] Conformational studies of microcystin-LR using NMR spectroscopy and molecular dynamic
Conformational studies of microcystin-LR using NMR spectroscopy and molecular dynamics calculations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformational studies of microcystin-LR using NMR spectroscopy and molecular dynamics calculations.
Biochemistry. 1996 Mar 12;35(10):3197-205
Authors: Trogen GB, Annila A, Eriksson J, Kontteli M, Meriluoto J, Sethson I, Zdunek J, Edlund U
NMR spectroscopy in aqueous and dimethyl sulfoxide/water solutions is used to determine the...
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[NMR paper] Conformational differences between complexes of elongation factor Tu studied 19F-NMR
Conformational differences between complexes of elongation factor Tu studied 19F-NMR spectroscopy.
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Eur J Biochem. 1993 Dec 15;218(3):1041-7
Authors: Eccleston JF, Molloy DP, Hinds MG, King RW, Feeney J
An analogue of elongation factor Tu (EF-Tu) from Escherichia coli was prepared by...
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[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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NMR resonance assignments of thrombin reveal the conformational and dynamic effects o
NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation
Lechtenberg, B. C., Johnson, D. J. D., Freund, S. M. V., Huntington, J. A....
The serine protease thrombin is generated from its zymogen prothrombin at the end of the coagulation cascade. Thrombin functions as...
Date: 2010-08-10
Source: PNAS
Number: 32