Allard P - Search Results

1

(13)C-(1)H NMR relaxation and fluorescence anisotropy decay study of tyrosine dynamics in motilin.

Damberg P, Jarvet J, Allard P, Mets U, Rigler R, Gräslund A. Damberg P, et al. Among authors: allard p. Biophys J. 2002 Nov;83(5):2812-25. doi: 10.1016/S0006-3495(02)75290-9. Biophys J. 2002. PMID: 12414713 Free PMC article.

2

Mapping of the spectral density function of a C alpha-H alpha bond vector from NMR relaxation rates of a 13C-labelled alpha-carbon in motilin.

Allard P, Jarvet J, Ehrenberg A, Gräslund A. Allard P, et al. J Biomol NMR. 1995 Feb;5(2):133-46. doi: 10.1007/BF00208804. J Biomol NMR. 1995. PMID: 7703699

3

Solution structure by 1H and dynamics by natural abundance 13C NMR of a receptor recognising peptide derived from a C-terminal fragment of neuropeptide Y.

Arvidsson K, Jarvet J, Allard P, Ehrenberg A. Arvidsson K, et al. Among authors: allard p. J Biomol NMR. 1994 Sep;4(5):653-72. doi: 10.1007/BF00404276. J Biomol NMR. 1994. PMID: 7919952

4

Spectral-Density Mapping of 13Calpha-1Halpha Vector Dynamics Using Dipolar Relaxation Rates Measured at Several Magnetic Fields.

Jarvet J, Allard P, Ehrenberg A, Graslund A. Jarvet J, et al. Among authors: allard p. J Magn Reson B. 1996 Apr;111(1):23-30. doi: 10.1006/jmrb.1996.0056. J Magn Reson B. 1996. PMID: 8661260

The spectral-density mapping of a 13Calpha-1Halpha vector of Leu10 in the 22-residue peptide hormone motilin [P. Allard, J. Jarvet, A. Ehrenberg, and A. Graslund, J. Biomol. NMR 5, 133-146 (1995)] is extended in this paper to three polarizing fields 9.4, 11.7, and 1 …

The spectral-density mapping of a 13Calpha-1Halpha vector of Leu10 in the 22-residue peptide hormone motilin [P. Allard, J. Ja …

5

Phase-Sensitive Two-Dimensional Heteronuclear Zero- and Double-Quantum-Coherence Spectroscopy.

Jarvet J, Allard P. Jarvet J, et al. Among authors: allard p. J Magn Reson B. 1996 Sep;112(3):240-4. doi: 10.1006/jmrb.1996.0137. J Magn Reson B. 1996. PMID: 8812911

6

Quantitative estimation of magnitude and orientation of the CSA tensor from field dependence of longitudinal NMR relaxation rates.

Damberg P, Jarvet J, Allard P, Gräslund A. Damberg P, et al. Among authors: allard p. J Biomol NMR. 1999 Sep;15(1):27-37. doi: 10.1023/A:1008308224556. J Biomol NMR. 1999. PMID: 20703961

7

NMR Relaxation Mechanisms for Backbone Carbonyl Carbons in a 13 C, 15 N-Labeled Protein.

Allard P, Härd T. Allard P, et al. J Magn Reson. 1997 May;126(1):48-57. doi: 10.1006/jmre.1997.1131. J Magn Reson. 1997. PMID: 9252275

8

Binding of the competitive inhibitor dCDP to ribonucleoside-diphosphate reductase from Escherichia coli studied by 1H NMR. Different properties of the large protein subunit and the holoenzyme.

Allard P, Kuprin S, Shen B, Ehrenberg A. Allard P, et al. Eur J Biochem. 1992 Sep 15;208(3):635-42. doi: 10.1111/j.1432-1033.1992.tb17229.x. Eur J Biochem. 1992. PMID: 1396671 Free article.

9

Solution structure of the SH3 domain from Bruton's tyrosine kinase.

Hansson H, Mattsson PT, Allard P, Haapaniemi P, Vihinen M, Smith CI, Hard T. Hansson H, et al. Among authors: allard p. Biochemistry. 1998 Mar 3;37(9):2912-24. doi: 10.1021/bi972409f. Biochemistry. 1998. PMID: 9485443

10

Studies on ribonucleoside-diphosphate reductase from Escherichia coli. The product dCDP is a competitive inhibitor and functions as a spectroscopic probe for the substrate binding site; demonstration by enzyme kinetics and 1H NMR.

Shen B, Allard P, Kuprin S, Ehrenberg A. Shen B, et al. Among authors: allard p. Eur J Biochem. 1992 Sep 15;208(3):631-4. doi: 10.1111/j.1432-1033.1992.tb17228.x. Eur J Biochem. 1992. PMID: 1396670 Free article.

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