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Article

A mutant T4 lysozyme displays five different crystal conformations.

Nature - 15 Nov 1990

Faber H R, Matthews B W

Abstract excerpt

Phage T4 lysozyme consists of two domains between which is formed the active-site cleft of the enzyme. The crystallographically determined thermal displacement parameters for the protein suggested that the amino terminal of the two domains undergoes 'hinge-bending' motion about an axis passing through the waist of the molecule. Such conformational mobility may be important in allowing access of substrates to the...

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PMID: 2234094
DOI: 10.1038/348263a0

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

A mutant T4 lysozyme displays five different crystal conformations.PMID 2234094Read ↗

Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.Semantic proximity Read ↗

Structure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3-->Pro.Semantic proximity Read ↗

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

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

Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions.Semantic proximity Read ↗

Crystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity.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 ↗

Molecular dynamics simulations of an engineered T4 lysozyme exclude helix to sheet transition, and provide insights into long distance, intra-protein switchable motion.Semantic proximity Read ↗

Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability.Semantic proximity Read ↗

Structure-based design of a lysozyme with altered catalytic activity.Semantic proximity Read ↗

Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His.Semantic proximity Read ↗

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

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