Biological Magnetic Resonance by Philip L. Yeagle (auth.), Lawrence J. Berliner, Jacques

By Philip L. Yeagle (auth.), Lawrence J. Berliner, Jacques Reuben (eds.)

We are happy to provide quantity nine of our hugely winning sequence, which now celebrates 12 years of offering the magnetic resonance neighborhood with topical, authoritative chapters on new points of organic magnetic resonance. As continually, we attempt to provide a range of subject insurance in every one quantity, starting from functions of in vivo magnetic resonance to extra basic facets of electron spin resonance and nuclear magnetic resonance. Philip Yeagle offers an eagerly awaited bankruptcy on 31p NMR experiences of membranes and membrane protein interactions. Alan Marshall has con­ tributed chapters to the amount: one, with Jiejun Wu, describes magnetic resonance stories of 5S-RNA as probes of its constitution and conformation; the secon

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Perhaps the different packing for the polar headgroups in small vesicles enhances the interaction between the lanthanide ion and the phosphate. It is also not clear what kind of membraneous structure is formed by hydrating phospholipids with buffers containing molar concentrations of trivalent cations. , 1979; Hope and Cullis, 1980). Substantial increases in the width of the 31p NMR powder pattern are well documented for calcium binding to phosphatidylserine. The effect is apparently to dehydrate the surface of that membrane, thereby producing a spectrum similar to those of dehydrated phospholipids.

However, one must be cautious in interpreting data involving phosphatidylserine, both because of the ease of oxidation of this phospholipid and because of the great affinity of the headgroup of phosphatidylserine for cations which, upon binding, are known to render the whole 36 Philip L. Yeagle membrane more rigid. Such an effect was noted earlier in studies of calcium binding to phosphatidylserine (Kohler and Klein, 1977). Since biological membranes consist of complex mixtures of phospholipids it is important to examine the behavior of phospholipids in the presence of other phospholipid classes.

T2 in pure phospholipid bilayers can be 10-20 msec, while in proteincontaining membranes T2 can be an order of magnitude shorter. This change in T2 has an effect on the 31p powder pattern, broadening portions of it so that the upfield maximum is less pronounced compared to the downfield shoulder. , 1981). The dramatic reduction in 31p T2 in the presence of membrane proteins is, at low to moderate levels of membrane protein, not accompanied by a change in T 1 • This indicates that headgroup rotational diffusion (the motion with the short correlation time) in the supraannular phospholipid is not significantly altered by the presence of membrane protein.

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