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

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

Protein science : a publication of the Protein Society - 1 May 2003

Mollah A K M M, Stennis Rhonda L, Mossing Michael C

Abstract excerpt

The thermodynamic stabilities of three monomeric variants of the bacteriophage lambda Cro repressor that differ only in the sequence of two amino acids at the apex of an engineered beta-hairpin have been determined. The sequences of the turns are EVK-XX-EVK, where the two central residues are DG, GG, and GT, respectively. Standard-state unfolding free energies, determined from circular dichroism measurements as a...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to DNA-Binding Proteins

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

Share to Protein Denaturation

Share to Protein Structure, Secondary

Share to Repressor Proteins

Share to Thermodynamics

Share to Viral Proteins

Share to Viral Regulatory and Accessory Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 12717034
DOI: 10.1110/ps.0239003
PMCID: PMC2323882

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Stability of monomeric Cro variants: Isoenergetic transformation of a type I' to a type II' beta-hairpin by single amino acid replacements.PMID 12717034Read ↗

Stable, monomeric variants of lambda Cro obtained by insertion of a designed beta-hairpin sequence.Semantic proximity Read ↗

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

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

Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks.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 ↗

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

Contribution of the dimeric state to the thermal stability of the flavoprotein D-amino acid oxidase.Semantic proximity Read ↗

Disulfide mutants of barnase. I: Changes in stability and structure assessed by biophysical methods and X-ray crystallography.Semantic proximity Read ↗

Helix-capping interaction in lambda Cro protein: a free energy simulation analysis.Semantic proximity Read ↗

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

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

Microsecond protein folding through a compact transition state.Semantic proximity Read ↗

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