Nuclear Magnetic Resonance of Biological Macromolecules, by Thomas L. James, Volker Dotsch, Uli Schmitz

By Thomas L. James, Volker Dotsch, Uli Schmitz

This quantity and its significant other, Volume 338, complement Volumes 176, 177, 239, and 261. Chapters are written with a "hands-on" standpoint. that's, sensible functions with serious reviews of methodologies and experimental issues had to layout, execute, and interpret NMR experiments pertinent to organic molecules.

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Extra resources for Nuclear Magnetic Resonance of Biological Macromolecules, Part B, Volume 339 (Methods in Enzymology)

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47M. A. Singer and S. Lindquist, Mol. CelL 1, 639 (1998). 32 PROTEINS [2] and inositol), all except inositol gave low preferential hydration. 28 The strong preferential hydration displayed by inositol was ascribed to its strongly hydrophilic character and its high degree of hydration. A m i n o acids, amino acid salts, and methylamines. Small neutral amino acids such as glycine, a-alanine, and /%alanine exhibit a concentration-independent degree of preferential hydration and therefore belong to the first class of protein structure stabilizers.

Natl. Acad. Sci. A. 95, 6705 (1998). 22 PROTEINS [21 were 15N-labeled. Both trans-splicing and chemical ligation approaches can be extended to allow three recombinant protein segments to be regioselectively linked together: the feasibility of joining three segments by chemical ligation has been demonstrated in a model synthetic peptide systeml2; trans-splicing has been used for selective isotope labeling of a central segment of maltose binding protein 8 and can be used to label selectively any segment between structurally flexible residues.

A. Horita, D. W. Farnsworth, and R. A. Byrd, J. Biol. NMR 16, 339 (2000). 16j. Freund and H. R. Kalbitzer, Z Biol. NMR 5, 321 (1995). net/elsonline. 18R. E. Godt and D. W. Maughan, Am. J. Physiol. 254, C591 (1988). 19D. Seidel and H. Schmidt-Gayk, in "Innere Medizin," 5th Ed. (G. ), pp. 548-562. Thieme, Stuttgart, 1980. 2 using KOH. The concentration of all the relevant ionic species are given in Table I. Inorganic phosphate is used as a substitute for all phosphate compounds in the cell, and acetate for all protein and metabolite carboxyl groups.

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