By Philip H. Bolton (auth.), Lawrence J. Berliner, Jacques Reuben (eds.)

We have now reached our 6th quantity in a chain which has slightly by accident develop into an annual occasion. whereas we nonetheless intend to supply a quantity provided that an appropriate variety of very good chapters within the vanguard of organic magnetic resonance can be found, our philosophy is to offer a pedagogical but serious description and overview of chosen subject matters in magazine­ netic resonance of present curiosity to the group of biomedical scien­ tists. This quantity fulfills our ambitions good. As constantly, we open the quantity with a bankruptcy which without delay addresses an in vivo organic challenge: Phil Bolton's presentation of latest recommendations in measuring 31 P NMR in cells. Lenkinski's bankruptcy at the conception and functions of lanthanides in protein reports covers the main points, highlights, and pitfalls of research of those com­ plexes in biochemical NMR. Reed and Markham summarize the interpreta­ tion of EPR spectra of manganese when it comes to constitution and serve as of proteins and enzymes. Dalton and associates describe the purposes to organic difficulties of the rather new potential of time area ESR. ultimately, we're happy to supply a departure from mainstream magnetic resonance with the great and stimulating bankruptcy by way of Gus Maki at the concept, instrumentation, and functions of optically detected magnetic resonance.

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Phys. Lett. 52:407. 2 Lanthanide Complexes of Peptides and Proteins Robert E. Lenkinski 1. INTRODUCTION The well-documented success of nuclear magnetic resonance (NMR) spectroscopy to provide configurational information about organic molecules has led to the application of this method to studies of peptides and proteins in solution (Dwek, 1972; James, 1975; Wuthrich, 1976; Jardetzky and Roberts, 1981). The potential structural information available from NMR spectroscopy is enormous since signals can be observed, in principle, from individual nuclei within a molecule, and the nature of these signals (chemical shift positions, coupling constants, and relaxation times) depends on the environment of each nucleus.

Therefore, the factoring of the relaxation rates obtained for shifting lanthanide ions can also be employed to calculate absolute distances between the metal ion and the nuclei being observed provided that a precise value for the electron spin relaxation time is known. Lee and Sykes -(1980a-d; 1981; 1982; 1983) have demonstrated the utility of this approach in their elegant analysis of the Yb(III)-induced relaxation rate enhancements of parvalbumin. 46 Ho Er Tm Yb • Ratios of the two contributions to.

101: 1080. Bolton, P. , 1981, J. Magn. Reson. 43:339. Bolton, P. , 1982a, Chern. Phys. Lett. 89: 139. Bolton, P. , 1982b, J. Magn. Reson. 46:306. Davies, D. , 1978, Prog. Nucl. Magn. Reson. Spectrosc. 12: 135. , and Ernst, R. , 1982, J. Am. Chern. Soc. 104:3731. , and Anderson, W. , 1963, J. Chern. Phys. 39:806. , 1979, Bull. Magn. Reson. 1 :5. , 1980, Biochirn. Biophys. Acta. 610:47. Hoult, D. , Busby, S. J. , Gadian, D. , Radda, G. , Richards, R. , and Seeley, P. , 1974, Nature (London) 253:285.

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