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

Repacking the Core of T4 lysozyme by automated design.

Journal of molecular biology - 19 Sept 2003

Mooers Blaine H M, Datta Deepshikha, Baase Walter A, Zollars Eric S, Mayo Stephen L, Matthews Brian W

Abstract excerpt

Automated protein redesign, as implemented in the program ORBIT, was used to redesign the core of phage T4 lysozyme. A total of 26 buried or partially buried sites in the C-terminal domain were allowed to vary both their sequence and side-chain conformation while the backbone and non-selected side-chains remained fixed. A variant with seven substitutions ("Core-7") was identified as having the most favorable...

Read the complete abstract on PubMed

Topics

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

Share to Automation
Share to Bacteriophage T4
Share to Enzyme Stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Methionine

Share to Muramidase

Share to Solvents

Share to Thermodynamics

Source

Identifiers

PMID: 12963380
DOI: 10.1016/s0022-2836(03)00856-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Repacking the Core of T4 lysozyme by automated design.PMID 12963380Read ↗

Automated selection of stabilizing mutations in designed and natural proteins.Semantic proximity Read ↗

What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties.Semantic proximity Read ↗

De novo design of the hydrophobic core of ubiquitin.Semantic proximity Read ↗

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

The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme.Semantic proximity Read ↗

Stabilization of the SARS-CoV-2 Receptor Binding Domain by Protein Core Redesign and Deep Mutational ScanningSemantic proximity Read ↗

Exploring subdomain cooperativity in T4 lysozyme I: structural and energetic studies of a circular permutant and protein fragment.Semantic proximity Read ↗

Stabilization of the SARS-CoV-2 receptor binding domain by protein core redesign and deep mutational scanning.Semantic proximity Read ↗

Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.Semantic proximity Read ↗

Sequence search methods and scoring functions for the design of protein structures.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 ↗

Robust folding of a de novo designed ideal protein even with most of the core mutated to valine.Semantic proximity Read ↗

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