By Philip H. Bolton (auth.), Lawrence J. Berliner, Jacques Reuben (eds.)
We have now reached our 6th quantity in a chain which has a bit by accident turn into an annual occasion. whereas we nonetheless intend to provide a quantity provided that an appropriate variety of first-class chapters within the leading edge of organic magnetic resonance can be found, our philosophy is to provide a pedagogical but serious description and evaluate of chosen themes in magazine netic resonance of present curiosity to the group of biomedical scien tists. This quantity fulfills our objectives good. As regularly, we open the quantity with a bankruptcy which without delay addresses an in vivo organic challenge: Phil Bolton's presentation of latest thoughts in measuring 31 P NMR in cells. Lenkinski's bankruptcy at the concept and purposes 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 by way of constitution and serve as of proteins and enzymes. Dalton and associates describe the purposes to organic difficulties of the rather new power of time area ESR. ultimately, we're happy to supply a departure from mainstream magnetic resonance with the excellent and stimulating bankruptcy by way of Gus Maki at the idea, instrumentation, and functions of optically detected magnetic resonance.
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Additional resources for Biological Magnetic Resonance: Volume 6
Maudsley, A. , and Ernst, R. , 1978, Chern. Phys. Lett. 55:9. Moon, R. , and Richards, J. , 1973, BioI. Chern. 248:7276. , 1979, J. Am. Chern. Soc. 101 :4481. , 1954, Phys. Rev. 96: 543. Shulman, R. , 1983, Sci. Am. 248:86. , and Ernst, R. , 1977, Chern. 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).
1974) for the Gd(III)-lysozyme complex at 25°C. 9 x 10- 9 s at 55°C. c is dominated by a contribution from the rotational correlation time. In using a single correlation time for lysozyme, we have assumed that neither anisotropic rotation nor internal motions are present. In cases where this assumption is not valid we suggest that the use of a single correlation time may still be adequate for the computation of absolute metal-proton distances. r results in much smaller errors in the distance. We have calculated these various distances for lysozyme, using the appropriate values of the various parameters in equation (26).
1979). Using a value of 5 x to- 10 M for the dissociation constant for the Yb(III) complex in conjunction with the kinetic data reported in Table 4 we arrive at an estimate of ca. 200 sec for r M, the lifetime of the Yb(III) complex. Using this value in equation (11) it is clear that parvalbumin is almost certainly in slow exchange between the free and Yb(III)-complexed state on the 1 H NMR chemical shift time scale. A Figure 3. 96. Temperature = 303 K. 5 mM DSS in D 2 0, pH 665.
Biological Magnetic Resonance: Volume 6 by Philip H. Bolton (auth.), Lawrence J. Berliner, Jacques Reuben (eds.)