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

Helix-capping interaction in lambda Cro protein: a free energy simulation analysis.

Proteins - 1 Aug 1994

Tidor B

Abstract excerpt

The stability mutant Tyr-26-->Asp was studied in the Cro protein from bacteriophage lambda using free energy molecular dynamics simulations. The mutant was calculated to be more stable than the wild type by 3.0 +/- 1.7 kcal/mol/monomer, in reasonable agreement with experiment (1.4 kcal/mol/monome...

Topics

Aspartic Acid
Bacteriophage lambda
Computer Simulation
DNA-Binding Proteins
Hydrogen Bonding
Models, Molecular
Mutation
Protein Structure, Secondary
Repressor Proteins
Thermodynamics
Tyrosine
Viral Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Viral Regulatory and Accessory Proteins

Water

Source

Identifiers

PMID: 7984627
DOI: 10.1002/prot.340190406

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7984627-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 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.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Helix-capping interaction in lambda Cro protein: a free energy simulation analysis.PMID 7984627Read ↗

Retroevolution of lambda Cro toward a stable monomer.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 ↗

Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices.Semantic proximity Read ↗

Stabilizing and destabilizing effects of placing beta-branched amino acids in protein alpha-helices.Semantic 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 ↗

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

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

Contribution of the hydrophobic effect to protein stability: analysis based on simulations of the Ile-96----Ala mutation in barnase.Semantic proximity Read ↗

Stability and solvation of Thr/Ser to Ala and Gly mutations at the N-cap of alpha-helices.Semantic proximity Read ↗

Terminal sidechain packing of a designed beta-hairpin influences conformation and stability.Semantic proximity Read ↗

Simulation analysis of the stability mutants R96H of bacteriophage T4 lysozyme and I96A of barnase.Semantic proximity Read ↗

A general acid-base mechanism for the stabilization of a tetrahedral adduct in a serine-carboxyl peptidase: a computational study.Semantic proximity Read ↗

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