@article {4080,
	title = {Specific N-15,NH correlations for residues in N-15,C-13 and fractionally deuterated proteins that immediately follow methyl-containing amino acids},
	journal = {Journal of Biomolecular Nmr},
	volume = {10},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: YG934Times Cited: 10Cited Reference Count: 47},
	month = {Oct},
	pages = {283-288},
	type = {Article},
	abstract = {A triple-resonance pulse scheme is described which records N-15, NH correlations of residues that immediately follow a methyl-containing amino acid. The experiment makes use of a N-15, C-13 and fractionally deuterated protein sample and selects for CH2D methyl types. The experiment is thus useful in the early stages of the sequential assignment process as well as for the confirmation of backbone N-15, NH chemical shift assignments at later stages of data analysis. A simple modification of the sequence also allows the measurement of methyl side-chain dynamics. This is particularly useful for studying side-chain dynamic properties in partially unfolded and unfolded proteins where the resolution of aliphatic carbon and proton chemical shifts is limited compared to that of amide nitrogens.},
	keywords = {C-13, C-13/N-15-ENRICHED PROTEINS, CELLULOSE-BINDING DOMAIN, correlations, H-2 spin relaxation, H-2-labeled proteins, ISOTOPICALLY-ENRICHED PROTEINS, LABELED PROTEINS, N-15, NH, NMR EXPERIMENTS, PERDEUTERATED PROTEINS, RELAXATION-TIMES, SEQUENTIAL ASSIGNMENT, SIDE-CHAIN, TRIPLE-RESONANCE EXPERIMENTS},
	isbn = {0925-2738},
	url = {<Go to ISI>://A1997YG93400009},
	author = {Muhandiram, D. R. and Johnson, P. E. and Yang, D. W. and Zhang, O. W. and McIntosh, L. P. and Kay, L. E.}
}
@article {3480,
	title = {AN AUTOCLAVABLE GLUCOSE BIOSENSOR FOR MICROBIAL FERMENTATION MONITORING AND CONTROL},
	journal = {Biotechnology and Bioengineering},
	volume = {46},
	number = {6},
	year = {1995},
	note = {ISI Document Delivery No.: QY630Times Cited: 16Cited Reference Count: 49},
	month = {Jun},
	pages = {514-524},
	type = {Article},
	abstract = {The design, construction, and characterization of a prototype-regenerable glucose biosensor based on the reversible immobilization of glucose oxidase (GOx) using cellulose binding domain (CBD) technology is described. GOx, chemically linked to CBD, is immobilized by binding to a cellulose matrix on the sensor-indicating electrode. Enzyme immobilization can be reversed by perfusing the cellulose matrix with a suitable eluting solution. An autoclavable sensor membrane system is employed which is shown to be practical for use in real microbial fermentations. The prototype glucose biosensor was used without failure or deterioration during fed-batch fermentations of Escherichia coli reaching a maximum cell density of 85 g (dry weight)/L. Medium glucose concentration based on sensor output correlated closely with off-line glucose analysis and was controlled manually at 0.44 +/- 0.2 g/L for 2 h based on glucose sensor output. The sensor enzyme component could be eluted and replaced without interrupting the fermentation. To our knowledge, no other in situ biosensor has been used for such an extended period of time in such a high-cell-density fermentation. (C) 1995 John Wiley \& Sons, Inc.},
	keywords = {(CBD), AMPEROMETRIC BIOSENSORS, BATCH, BIOSENSOR, CELLULOSE BINDING DOMAIN, CELLULOSE-BINDING DOMAIN, ELECTROCHEMICAL DETECTOR, ENZYME ELECTRODE, ESCHERICHIA-COLI, FERMENTATION MONITORING, FLOW-INJECTION ANALYSIS, GLUCOSE BIOSENSOR, GLUCOSE OXIDASE, OPTIMIZATION, OXIDASE ELECTRODE, OXYGEN},
	isbn = {0006-3592},
	url = {<Go to ISI>://A1995QY63000003},
	author = {Phelps, M. R. and Hobbs, J. B. and Kilburn, D. G. and Turner, R. F. B.}
}
