NMR and enzymology of modified DNA/protein interactions

Conference · Fri Dec 30 23:00:00 EST 1994

OSTI ID:134860

Kennedy, M A ^[1]

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1. Battelle Pacific Northwest Lab., Richland, WA (United States)

We have found distinct DNA structure and base dynamics precisely at the TpA cleavage site in the TTTAAA AHA III endonuclease restriction sequence. Hence, the unusual base stacking and mobility found in this sequence may be important to the mechanism of enzymatic cleavage of the phophodiester bond.

• Research Organization: New York Academy of Sciences, New York, NY (United States)
• DOE Contract Number: FG06-89ER75522
• OSTI ID: 134860
• Report Number(s): CONF-9307221--
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
ADENINES
BASES
CLEAVAGE
DETECTION
DNA
DNA SEQUENCING
DYNAMICS
ENDONUCLEASES
ENZYMES
METHYLATION
NMR IMAGING
PHOSPHODIESTERASES
PROTEINS
STRUCTURE-ACTIVITY RELATIONSHIPS