DNA polymerase I (Klenow fragment): Role of the structure and length of a template in enzyme recognition

FEBS Letters

Volumn 248, Issue 1-2, 1989, Pages 97-100

  Kolocheva, T I ^a   Nevinsky, G A ^a   Volchkova, V A ^a   Levina, A S ^a   Khomov, V V ^b   Lavrik, O I ^a  

^a INSTITUTE OF CHEMICAL BIOLOGY AND FUNDAMENTAL MEDICINE   (Russian Federation)

^b STATE RESEARCH CENTER OF VIROLOGY AND BIOTECHNOLOGY VECTOR   (Russian Federation)

Author keywords

DNA polymerase I; Klenow fragment; Protein nucleic acid interaction

Indexed keywords

DNA POLYMERASE; PROTEIN;

HUMAN; PRIORITY JOURNAL; TEMPLATE;

DNA; DNA POLYMERASE I; DNA-DIRECTED DNA POLYMERASE; ELECTROCHEMISTRY; HYDROGEN BONDING; KINETICS; MODELS, THEORETICAL; MOLECULAR STRUCTURE; OLIGONUCLEOTIDES; PEPTIDE FRAGMENTS; SUPPORT, NON-U.S. GOV'T; TEMPLATES, GENETIC;

EID: 0024506495     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/0014-5793(89)80439-9     Document Type: Article

References (12)

1. [Klenow fragment of DNA-polymerase I from E. coli. III. The role of internucleotide phosphate groups of the matrix in its binding with the enzyme].
2. NMR studies of the conformations and interactions of substrates and ribonucleotide templates bound to the large fragment of DNA polymerase I