Operator DNA sequence variation enhances high affinity binding by hinge helix mutants of lactose repressor protein.

doi:10.1021/bi000924z

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Operator DNA sequence variation enhances high affinity binding by hinge helix mutants of lactose repressor protein.

Biochemistry - 12 Sept 2000

Falcon C M, Matthews K S

Abstract excerpt

The mechanism by which genetic regulatory proteins discern specific target DNA sequences remains a major area of inquiry. To explore in more detail the interplay between DNA and protein sequence, we have examined binding of variant lac operator DNA sequences to a series of mutant lactose repressor proteins (LacI). These proteins were altered in the C-terminus of the hinge region that links the N-terminal DNA...

Topics

Bacterial Proteins
Base Pairing
DNA, Bacterial
Escherichia coli
Escherichia coli Proteins
Genetic Variation
Glycine
Lac Repressors
Lactose
Mutagenesis, Site-Directed
Operator Regions, Genetic
Protein Binding
Protein Structure, Secondary
Repressor Proteins
Sequence Analysis, DNA
Temperature

Source

Open in PubMed

Identifiers

PMID: 10998245
DOI: 10.1021/bi000924z

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics