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

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

Biochemistry - 23 Jul 1991

Sun D P, Sauer U, Nicholson H, Matthews B W

Abstract excerpt

Six designed mutants of T4 lysozyme were created in an attempt to create putative salt bridges on the surface of the protein. The first three of the mutants, T115E (Thr 115 to Glu), Q123E, and N144E, were designed to introduce a new charged side chain close to one or more existing charged groups of the opposite sign on the surface of the protein. In each of these cases the putative electrostatic interactions...

Read the complete abstract on PubMed

Topics

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

Share to Hydrogen-Ion Concentration
Share to Models, Molecular
Share to Muramidase

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

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Protein Conformation

Share to Protein Engineering

Share to X-Ray Diffraction

Source

Identifiers

PMID: 1854726
DOI: 10.1021/bi00243a015

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

Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.PMID 1854726Read ↗

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

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 ↗

Structural and genetic analysis of electrostatic and other interactions in bacteriophage T4 lysozyme.Semantic proximity Read ↗

Structure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme.Semantic proximity Read ↗

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

Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein.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 ↗

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

Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme.Semantic proximity Read ↗

Increasing protein stability by polar surface residues: domain-wide consequences of interactions within a loop.Semantic proximity Read ↗

Salt bridges in the hyperthermophilic protein Ssh10b are resilient to temperature increases.Semantic proximity Read ↗

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