Structure and function of type II restriction endonucleases
A Pingoud, A Jeltsch - Nucleic acids research, 2001 - academic.oup.com
More than 3000 type II restriction endonucleases have been discovered. They recognize
short, usually palindromic, sequences of 4–8 bp and, in the presence of Mg2+, cleave the …
short, usually palindromic, sequences of 4–8 bp and, in the presence of Mg2+, cleave the …
Recognition and cleavage of DNA by type‐II restriction endonucleases
A Pingoud, A Jeltsch - European Journal of Biochemistry, 1997 - Wiley Online Library
Restriction endonucleases are enzymes which recognize short DNA sequences and cleave
the DNA in both strands. Depending on the enzymological properties different types are …
the DNA in both strands. Depending on the enzymological properties different types are …
Coupling of local folding to site-specific binding of proteins to DNA
RS Spolar, MT Record Jr - Science, 1994 - science.org
Thermodynamic studies have demonstrated the central importance of a large negative heat
capacity change (Δ C° assoc) in site-specific protein-DNA recognition. Dissection of the …
capacity change (Δ C° assoc) in site-specific protein-DNA recognition. Dissection of the …
DNA and RNA cleavage by metal complexes
G Pratviel, J Bernadou, B Meunier - Advances in Inorganic Chemistry, 1998 - Elsevier
Publisher Summary This chapter discusses DNA and RNA cleavage by metal complexes.
DNA and RNA cleavage, a very active field of research, has been developed in two main …
DNA and RNA cleavage, a very active field of research, has been developed in two main …
The crystal structure of EcoRV endonuclease and of its complexes with cognate and non‐cognate DNA fragments.
FK Winkler, DW Banner, CH Oefner… - The EMBO …, 1993 - embopress.org
The crystal structure of EcoRV endonuclease has been determined at 2.5 A resolution and
that of its complexes with the cognate DNA decamer GGGATATCCC (recognition sequence …
that of its complexes with the cognate DNA decamer GGGATATCCC (recognition sequence …
Structure of Bam HI endonuclease bound to DNA: partial folding and unfolding on DNA binding
M Newman, T Strzelecka, LF Dorner, I Schildkraut… - Science, 1995 - science.org
The crystal structure of restriction endonuclease Bam HI complexed to DNA has been
determined at 2.2 angstrom resolution. The DNA binds in the cleft and retains a B-DNA type …
determined at 2.2 angstrom resolution. The DNA binds in the cleft and retains a B-DNA type …
DNase I-induced DNA conformation: 2 Å structure of a DNase I-octamer complex
A Lahm, D Suck - Journal of molecular biology, 1991 - Elsevier
The structure of a complex between DNase I and d (GCGATCGC) 2 has been solved by
molecular replacement and refined to an R-factor of 0· 174 for all data between 6 and 2 Å …
molecular replacement and refined to an R-factor of 0· 174 for all data between 6 and 2 Å …
Restriction endonucleases and modification methylases
JE Anderson - Current Opinion in Structural Biology, 1993 - Elsevier
Restriction endonucleases and modification methylases offer excellent systems for studying
protein-DNA interactions. The past year has seen the experimental verification of some …
protein-DNA interactions. The past year has seen the experimental verification of some …
Protein—DNA recognition complexes: Conservation of structure and binding energy in the transition state
L Jen‐Jacobson - Biopolymers: Original Research on …, 1997 - Wiley Online Library
This paper considers how enzymes that catalyze reactions at specific DNA sites have been
engineered to overcome the problem of competitive inhibition by excess nonspecific binding …
engineered to overcome the problem of competitive inhibition by excess nonspecific binding …
Mg2+ Binding to the Active Site of EcoRV Endonuclease: A Crystallographic Study of Complexes with Substrate and Product DNA at 2-. ANG. Resolution
D Kostrewa, FK Winkler - Biochemistry, 1995 - ACS Publications
Revised Manuscript Received October 27, 1994® abstract: The type II restriction
endonuclease EcoRV was crystallized as a complex with the substrate DNA undecamer …
endonuclease EcoRV was crystallized as a complex with the substrate DNA undecamer …