PMID:11304669
| Citation |
Sugimoto, N (2000) DNA recognition of a 24-mer peptide derived from RecA protein. Biopolymers 55:416-24 |
|---|---|
| Abstract |
A novel 24-residue peptide (L2-G), Ile-Arg-Met-Lys-Ile-Gly-Val-Met-Phe-Gly-Asn-Pro-Glu-Thr-Thr-Thr-Gly-Gly-Asn-Ala-Leu-Lys-Phe-Tyr, derived from RecA can discriminate a single-stranded DNA (ssDNA) from a double-stranded DNA (dsDNA) and a new developed support with this peptide recognizes not dsDNA but ssDNA. The 24-mer peptide with L2 and helix G amino acids of Escherichia coli RecA protein showed the ssDNA binding property with more than 1000 times affinity difference for the dsDNA. However, truncated 15-mer peptide showed no ssDNA binding activity. In the ssDNA binding, L2-G changed its conformation with the perturbation of an alpha-helix structure. The ssDNA binding and the DNA discrimination property of this peptide were due to almost all L2 and helix G amino acids, respectively. This result is useful to design synthetic peptides as functional materials for DNA recognition. |
| Links |
PubMed Online version:<416::AID-BIP1017>3.0.CO;2-P 10.1002/1097-0282(2000)55:6<416::AID-BIP1017>3.0.CO;2-P |
| Keywords |
Amino Acid Sequence; Animals; Binding Sites; Chromatography, Affinity; Circular Dichroism; DNA/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Molecular Sequence Data; Molecular Structure; Nucleic Acid Conformation; Peptides/chemical synthesis; Peptides/chemistry; Peptides/metabolism; Protein Binding; Protein Conformation; Rec A Recombinases/chemistry; Rec A Recombinases/genetics; Rec A Recombinases/metabolism |
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