Discover Community Create You

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

Article

Computer-aided discrimination between active and inactive mutants of the N-terminal domain of the bacteriophage lambda repressor.

Journal of molecular biology - 1 Mar 1996

Kombo D C, Némethy G, Gibson K D, Rackovsky S, Scheraga H A

Abstract excerpt

Binding of the N-terminal domain of the lambda repressor to DNA is coupled to dimerization. Hydrophobic interactions between helix-5 and helix-5' drive the packing at the dimer interface. We have carried out computations of the conformational energy of packing of the fifth helices (and of the helix-4-loop-helix-5 portions) of variants of the lambda repressor operator binding domain, using an ECEPP/3-based packing...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA
Share to DNA-Binding Proteins
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Binding

Share to Protein Conformation

Share to Repressor Proteins

Share to Viral Proteins

Source

Identifiers

PMID: 8604135
DOI: 10.1006/jmbi.1996.0105

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Computer-aided discrimination between active and inactive mutants of the N-terminal domain of the bacteriophage lambda repressor.PMID 8604135Read ↗

The role of internal packing interactions in determining the structure and stability of a protein.Semantic proximity Read ↗

Structural and energetic consequences of disruptive mutations in a protein core.Semantic proximity Read ↗

Effectiveness of Φ-value analysis in the binding process of Arc repressor dimer.Semantic proximity Read ↗

Computational and experimental probes of symmetry mismatches in the Arc repressor-DNA complex.Semantic proximity Read ↗

The DNA binding arm of lambda repressor: critical contacts from a flexible region.Semantic proximity Read ↗

MIAX: a system for assessment of macromolecular interaction. 3) A parallel hybrid GA for flexible protein docking.Semantic proximity Read ↗

Effect of mutation at the interface of Trp-repressor dimeric protein: a steered molecular dynamics simulation.Semantic proximity Read ↗

A comparative three-dimensional model of the carboxy-terminal domain of the lambda repressor and its use to build intact repressor tetramer models bound to adjacent operator sites.Semantic proximity Read ↗

Functionally acceptable substitutions in two alpha-helical regions of lambda repressor.Semantic proximity Read ↗

Isolation of lambda repressor mutants with defects in cooperative operator binding.Semantic proximity Read ↗

Structure of solvation water around the active and inactive regions of a type III antifreeze protein and its mutants of lowered activity.Semantic proximity Read ↗

Binding sites of different geometries for the 16-3 phage repressor.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.