In vitro selection of RNase P RNA reveals optimized catalytic activity in a highly conserved structural domain.
Frank, D N
In vitro selection of RNase P RNA reveals optimized catalytic activity in a highly conserved structural domain. [electronic resource] - RNA (New York, N.Y.) Dec 1996 - 1179-88 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
1355-8382
Base Sequence
Binding Sites
Catalysis
Cloning, Molecular
Endoribonucleases--chemistry
Escherichia coli--enzymology
Escherichia coli Proteins
Gene Library
Genetic Variation
Molecular Sequence Data
Nucleic Acid Conformation
RNA Precursors--metabolism
RNA, Catalytic--chemistry
RNA, Transfer--genetics
Ribonuclease P
In vitro selection of RNase P RNA reveals optimized catalytic activity in a highly conserved structural domain. [electronic resource] - RNA (New York, N.Y.) Dec 1996 - 1179-88 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
1355-8382
Base Sequence
Binding Sites
Catalysis
Cloning, Molecular
Endoribonucleases--chemistry
Escherichia coli--enzymology
Escherichia coli Proteins
Gene Library
Genetic Variation
Molecular Sequence Data
Nucleic Acid Conformation
RNA Precursors--metabolism
RNA, Catalytic--chemistry
RNA, Transfer--genetics
Ribonuclease P