Activated Carbon by Hassler J.W.

By Hassler J.W.

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Both sample preparation methodologies and pulse sequences appear to be generally applicable, and many direct analogies to the solution of NMR structure determination process are evident. It is therefore reasonable to expect that de novo assignments will become more common in the near future, as commercial instrumentation and pulse programs are now available for this purpose. 139 However, to determine a global fold, a protein requires a significant number of experimentally determined, long-range internuclear distances.

Chem. , 118, 9255, 1996. 149. Hong, M. , Selective and extensive C-13 labeling of a membrane protein for solid-state NMR investigations, J. Biomol. NMR, 14, 71, 1999. 150. , Rehbein, K. , Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy, Nature, 420, 98, 2002. 151. , Rehbein, K. , Determination of solid-state NMR structures of proteins by means of three-dimensional N15-C-13-C-13 dipolar correlation spectroscopy and chemical shift analysis, Biochemistry, 42, 11476, 2003.

7, 211, 1996. 98. L. E. , Propagating structure of Alzheimer’s β,-Amyloid(10) is parallel β-sheet with residues in exact register, Proc. Natl. Acad. Sci. USA, 95, 13407, 1998. 99. C. , Dipolar recoupling NMR of biomolecular selfassemblies: determining inter- and intrastrand distances in fibrilized Alzheimer’s βamyloid peptide, Solid State Nucl. Magn. , 13, 149, 1998. 100. E. , Two-dimensional structure of β,-amyloid(10) fibrils, Biochemistry, 39, 3491, 2000. 101. S. , A peptide that inhibits hydroxyapatite growth is in an extended conformation on the crystal surface, Proc.

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