Peptides nuclear magnetic resonance

Greenfield, N. J., Montelione, G. T., Farid, R. S., and Hitchcock-DeGregori, S. E. (1998). The structure of the N-terminus of striated muscle a-tropomyosin in a chimeric peptide Nuclear magnetic resonance structure and circular dichroism studies. 

Urry, D. W. Nuclear magnetic resonance and the conformation of membrane-active peptides. In Enzymes of Biological Membranes, Vol. 1, (ed. Martonosi, A ), p. 31, Plenum Publishing Corp., New York 1976... 

Balaram, P., Bothner-By, A. A., Breslow, E. Nuclear magnetic resonance smdies of interaction of peptides and hormones with bovine neurophysin. Biochemistry 1973, 12, 4695 704. 

B Weinstein, AE Pritchard. Amino-acids and Peptides. Part XXVIII. Determination of racemization in peptide synthesis by nuclear magnetic resonance spectroscopy. J Chem Soc Perkin Trans 1, 1015, 1972. 

JS Davies, RJ Thomas, MK Williams. Nuclear magnetic resonance spectra of ben-zoyldipeptide esters. A convenient test for racemisation in peptide synthesis. J Chem Soc Chem Commun 76, 1975. 

Kamel AM, Zandi KS, Massefski WW. 2003. Identification of the degradation product of ezlopitant, a non-peptidic substance P antagonist receptor, by hydrogen deuterium exchange, electrospray ionization tandem mass spectrometry (ESI/MS/MM) and nuclear magnetic resonance (NMR) spectroscopy. J Pharm Biomed Anal 31 1211. 

Nuclear Magnetic Resonance Spectroscopy of Amino Acids, Peptides, and Proteins... 

In addition, any rational approach to peptide hormone and neurotransmitter design must ultimately depend on the application of physical-chemical principles of conformation and structure, the use of various spectroscopic methods (especially nuclear magnetic resonance, circular dlchrolsm, and Raman spectroscopies. X-ray analysis where possible, etc.), and an understanding of the nature of a hormone-receptor Interaction In physical-chemical terms. Here again the use of conformatlonally restricted peptide structures Is critical (, 2. Recently we have... 

C. Dhalluin, C. Boutillon, A. Tartar and G. Lippens, Magic angle spinning nuclear magnetic resonance in solid-phase peptide synthesis, J. Am. Chem. Soc., 1997, 119, 10494-10500. 

J. H. Davis, M. Auger and R. S. Hodges, High resolution 111 nuclear magnetic resonance of a transmembrane peptide, Biophys. J., 1995, 69, 1917-1932. 

Approaches are described in this paper to the deduction of peptide conformation in solution by the use of three techniques 13C nuclear magnetic resonance, conformational energy calculations, and circular dlchroism. Sections of this paper illustrate the types of conformational information that can be derived from each of the individual methods for the synthetic and naturally occurring cyclic peptides. For complete conformational analysis, however, a combination of techniques is usually necessary. 

The dependence of the principal components of the nuclear magnetic resonance (NMR) chemical shift tensor of non-hydrogen nuclei in model dipeptides is investigated. It is observed that the principal axis system of the chemical shift tensors of the carbonyl carbon and the amide nitrogen are intimately linked to the amide plane. On the other hand, there is no clear relationship between the alpha carbon chemical shift tensor and the molecular framework. However, the projection of this tensor on the C-H vector reveals interesting trends that one may use in peptide secondary structure determination. Effects of hydrogen bonding on the chemical shift tensor will also be discussed. The dependence of the chemical shift on ionic distance has also been studied in Rb halides and mixed halides. Lastly, the presence of motion can have dramatic effects on the observed NMR chemical shift tensor as illustrated by a nitrosyl meso-tetraphenyl porphinato cobalt (III) complex. 

Peptide Conformations. I. Nuclear Magnetic Resonance Study of the Carbamate Reaction of Amino Acids and Peptides, R. U. Lemieux and M. A. Barton, Can. J. Chem., 49 (1971) 767-776. 

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