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

Packing interface energetics in different crystal forms of the λ Cro dimer.

Proteins - 1 Jul 2014

Ahlstrom Logan S, Miyashita Osamu

Abstract excerpt

Variation among crystal structures of the λ Cro dimer highlights conformational flexibility. The structures range from a wild type closed to a mutant fully open conformation, but it is unclear if each represents a stable solution state or if one may be the result of crystal packing. Here we use molecular dynamics (MD) simulation to investigate the energetics of crystal packing interfaces and the influence of...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Molecular Dynamics Simulation
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation

Share to Protein Subunits

Share to Repressor Proteins

Share to Viral Regulatory and Accessory Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 24218107
DOI: 10.1002/prot.24478
PMCID: PMC4018431

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

Packing interface energetics in different crystal forms of the λ Cro dimer.PMID 24218107Read ↗

Two structures of a lambda Cro variant highlight dimer flexibility but disfavor major dimer distortions upon specific binding of cognate DNA.Semantic proximity Read ↗

Retroevolution of lambda Cro toward a stable monomer.Semantic proximity Read ↗

A trade between similar but nonequivalent intrasubunit and intersubunit contacts in Cro dimer evolution.Semantic proximity Read ↗

Molecular Mechanisms of Gain-of-Function Mutations in λ Cro Revealed by Molecular Dynamics SimulationsSemantic proximity Read ↗

Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding II: cooperative interactions of cro dimers.Semantic proximity Read ↗

The structural basis for enhanced stability and reduced DNA binding seen in engineered second-generation Cro monomers and dimers.Semantic proximity Read ↗

Electrostatic Interactions at the Dimer Interface Stabilize the E. coli β Sliding Clamp.Semantic proximity Read ↗

Structural response to mutation at a protein-protein interface.Semantic proximity Read ↗

Effects of salt bridges on protein structure and design.Semantic proximity Read ↗

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

Subunit interface dynamics in hexadecameric rubisco.Semantic proximity Read ↗

Stability of monomeric Cro variants: Isoenergetic transformation of a type I' to a type II' beta-hairpin by single amino acid replacements.Semantic proximity Read ↗

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