ArticlePLoS computational biology2012
Changes in Lysozyme Flexibility upon Mutation Are Frequent, Large and Long-Ranged.
Article in PLoS computational biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 47 citations in OpenAlex.
- Effects of Amino Acid Point Mutations on the Local Hydrophobicity, Structural Stability, and Conformational Flexibility of P-Glycoprotein.Biomolecules · 2026Article
- Enzyme stabilisation due to incorporation of a fluorinated non-natural amino acid at the protein surface.Scientific reports · 2024Article
- Unraveling Extremely DamagingJournal of personalized medicine · 2023Article
- Analyses of Mutation Displacements from Homology Models.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Emerging Mutations in Nsp1 of SARS-CoV-2 and Their Effect on the Structural Stability.Pathogens (Basel, Switzerland) · 2021Article
- Clustering of atomic displacement parameters in bovine trypsin reveals a distributed lattice of atoms with shared chemical properties.Scientific reports · 2019Article
- Rigidity and flexibility characteristics of DD[E/D]-transposases Mos1 and Sleeping Beauty.Proteins · 2019Article
- Coupled molecular dynamics mediate long- and short-range epistasis between mutations that affect stability and aggregation kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Hotspot for Disease-Associated Variants of Human PGM1 Is Associated with Impaired Ligand Binding and Loop Dynamics.Structure (London, England : 1993) · 2018Article
- Mutations in Antibody Fragments Modulate Allosteric Response Via Hydrogen-Bond Network Fluctuations.Biophysical journal · 2016Article
- Application of Rigidity Theory to the Thermostabilization of Lipase A from Bacillus subtilis.PLoS computational biology · 2016Article
- Unraveling the Deleterious Effects of Cancer-Driven STK11 Mutants Through Conformational Sampling Approach.Cancer informatics · 2016Article
- Rigidity Emerges during Antibody Evolution in Three Distinct Antibody Systems: Evidence from QSFR Analysis of Fab Fragments.PLoS computational biology · 2015Article
- Flexibility Correlation between Active Site Regions Is Conserved across Four AmpC β-Lactamase Enzymes.PloS one · 2015Article
- Thermodynamic stability and flexibility characteristics of antibody fragment complexes.Protein and peptide letters · 2014Article
- Towards comprehensive analysis of protein family quantitative stability-flexibility relationships using homology models.Methods in molecular biology (Clifton, N.J.) · 2014Article
- A case study comparing quantitative stability-flexibility relationships across five metallo-β-lactamases highlighting differences within NDM-1.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Punctuated evolution of influenza virus neuraminidase (A/H1N1) under opposing migration and vaccination pressures.BioMed research international · 2014Article
- Redistribution of flexibility in stabilizing antibody fragment mutants follows Le Châtelier's principle.PloS one · 2014Article
- In-silico screening of cancer associated mutation on PLK1 protein and its structural consequences.Journal of molecular modeling · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We investigate changes in human c-type lysozyme flexibility upon mutation via a Distance Constraint Model, which gives a statistical mechanical treatment of network rigidity. Specifically, two dynamical metrics are tracked. Changes in flexibility index quantify differences within backbone flexibility, whereas changes in the cooperativity correlation quantify differences within pairwise mechanical couplings. Regardless of metric, the same general conclusions are drawn. That is, small structural perturbations introduced by single point mutations have a frequent and pronounced affect on lysozyme flexibility that can extend over long distances. Specifically, an appreciable change occurs in backbone flexibility for 48% of the residues, and a change in cooperativity occurs in 42% of residue pairs. The average distance from mutation to a site with a change in flexibility is 17-20 Å. Interestingly, the frequency and scale of the changes within single point mutant structures are generally larger than those observed in the hen egg white lysozyme (HEWL) ortholog, which shares 61% sequence identity with human lysozyme. For example, point mutations often lead to substantial flexibility increases within the β-subdomain, which is consistent with experimental results indicating that it is the nucleation site for amyloid formation. However, β-subdomain flexibility within the human and HEWL orthologs is more similar despite the lowered sequence identity. These results suggest compensating mutations in HEWL reestablish desired properties.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.