NMR studies of complexes of L.casei dihydrofolate reductase with antifolate drugs: multiple conformation and conformational selection of bound rotational isomers

By: Feeney, JMaterial type: Text

TextReference number:a8414

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Item type	Current library	Collection	Class number	Copy number	Status	Date due	Barcode	Item reservations
Magazine	Staff publications New Materials Shelf	Non-fiction	XX(8414.1) (Browse shelf(Opens below))	1	Available		8414-1001

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Previous	XX(8411.1) Homologies between the contiguous and fragmented rRNAs of the two Plasmodium falciparum extrachromosomal DNAs are limited to core sequences	XX(8412.1) Development of high resolution NMR spectroscopy as a structural tool	XX(8413.1) NMR studies of dynamic processes and multiple conformation in protein ligand complexes	XX(8414.1) NMR studies of complexes of L.casei dihydrofolate reductase with antifolate drugs: multiple conformation and conformational selection of bound rotational isomers	XX(8415.1) NMR studies of interactions of ligands with dihydrofolate reductase	XX(8416.1) Deceptively simple exchange effects in homonuclear Hartmann-Hahn (HOHAHA) spectra of protein-ligand complexes	XX(8417.1) NMR studies of protein-ligand interactions	Next

In: Bioorganic chemistry in health care and technology by Pandit, U. K. and Alderweieldt, R. C. (editors), pp 109-120.

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