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

Structural and genetic analysis of electrostatic and other interactions in bacteriophage T4 lysozyme.

Ciba Foundation symposium - 1 Jan 1991

Dao-pin S, Nicholson H, Baase W A, Zhang X J, Wozniak J A, Matthews B W

Abstract excerpt

The lysozyme from bacteriophage T4 is being used as a model system to determine the roles of individual amino acids in the folding and stability of a typical globular protein. Such studies can provide quantitative information on the contributions made by different types of interactions including hydrogen bonds, hydrophobic interactions, salt bridges and disulphide bridges. To determine the contribution of...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Stability
Share to Models, Chemical
Share to Models, Molecular

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

Share to Muramidase

Share to Mutation

Share to Protein Conformation

Share to Surface Properties

Share to T-Phages

Source

Identifiers

PMID: 1814696
DOI: 10.1002/9780470514146.ch4

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

Structural and genetic analysis of electrostatic and other interactions in bacteriophage T4 lysozyme.PMID 1814696Read ↗

Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.Semantic proximity Read ↗

Electrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges.Semantic proximity Read ↗

Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation.Semantic proximity Read ↗

Lessons from the lysozyme of phage T4.Semantic proximity Read ↗

The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect.Semantic proximity Read ↗

The introduction of strain and its effects on the structure and stability of T4 lysozyme.Semantic proximity Read ↗

Relative importance of secondary structure and solvent accessibility to the stability of protein mutants. A case study with amino acid properties and energetics on T4 and human lysozymes.Semantic proximity Read ↗

Substitution with selenomethionine can enhance the stability of methionine-rich proteins.Semantic proximity Read ↗

Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent.Semantic proximity Read ↗

Correlation between mutational destabilization of phage T4 lysozyme and increased unfolding rates.Semantic proximity Read ↗

Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences.Semantic proximity Read ↗

Role of medium- and long-range interactions to the stability of the mutants of T4 lysozyme.Semantic proximity Read ↗

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