Search results for "Single amino acid"

showing 3 items of 3 documents

Short hydrogen bonds enhance nonaromatic protein-related fluorescence

2021

Significance Intrinsic fluorescence of nonaromatic amino acids is a puzzling phenomenon with an enormous potential in biophotonic applications. The physical origins of this effect, however, remain elusive. Herein, we demonstrate how specific hydrogen bond networks can modulate fluorescence. We highlight the key role played by short hydrogen bonds, present in the protein structure, on the ensuing fluorescence. We provide detailed experimental and molecular evidence to explain these unusual nonaromatic optical properties. Our findings should benefit the design of novel optically active biomaterials for applications in biosensing and imaging.

Chemical transformationOptics and PhotonicsGlutamineIntrinsic fluorescenceMolecular Dynamics SimulationPhotochemistryFluorescenceAb initio molecular dynamicsAmmoniaHumansSingle amino acidshort hydrogen bondDensity Functional TheoryMultidisciplinaryHydrogen bondChemistryintrinsic fluorescenceultraviolet fluorescenceHydrogen BondingConical intersectionFluorescenceBiophysics and Computational BiologyExcited statePhysical Sciences408PeptidesProceedings of the National Academy of Sciences of the United States of America
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Poly-Xaa Sequences in Proteins - Biological Role and Interactions with Metal Ions: Chemical and Medical Aspects

2016

Background: The understanding of the bioinorganic and coordination chemistry of metalloproteins containing unusual poly-Xaa sequences, in which a single amino acid is repeated consecutively, is crucial for describing their metal binding-structure-function relationship, and therefore also crucial for understanding their medicinal potential. To the best of our knowledge, this is the first systematic review on metal complexes with polyXaa sequences. Methods: We performed a thorough search of high quality peer reviewed literature on poly-Xaa type of sequences in proteins, focusing on their biological importance and on their interactions with metal ions. Results: 228 papers were included in the…

Metal ions in aqueous solutionComputational biology010402 general chemistry01 natural sciencesBiochemistryCoordination complexTurn (biochemistry)metal chaperonesCoordination ComplexesDrug DiscoveryMetalloproteinHumansAmino Acid SequenceSingle amino acidAmino AcidsBinding siteantimicrobial therapeuticsIonsPharmacologychemistry.chemical_classification010405 organic chemistryMetal bindingOrganic Chemistrymetal ionsProteinsBioinorganic chemistry0104 chemical scienceschemistryChemical physicsMetal-protein complexespoly-Xaa peptide sequencesMolecular MedicineCurrent Medicinal Chemistry
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Globally defining the effects of mutations in a picornavirus capsid

2021

The capsids of non-enveloped viruses are highly multimeric and multifunctional protein assemblies that play key roles in viral biology and pathogenesis. Despite their importance, a comprehensive understanding of how mutations affect viral fitness across different structural and functional attributes of the capsid is lacking. To address this limitation, we globally define the effects of mutations across the capsid of a human picornavirus. Using this resource, we identify structural and sequence determinants that accurately predict mutational fitness effects, refine evolutionary analyses, and define the sequence specificity of key capsid-encoded motifs. Furthermore, capitalizing on the derive…

PicornavirusViral proteinQH301-705.5Sciencevirusesmedicine.medical_treatmentPicornaviridaeComputational biologymedicine.disease_causeGenomeGeneral Biochemistry Genetics and Molecular BiologyVirusImmune systemcapsidmedicineSingle amino acidBiology (General)GeneTropismHost proteinGeneticsEvolutionary BiologyMicrobiology and Infectious DiseaseMutationmutational fitness effectsProteaseGeneral Immunology and MicrobiologybiologyGeneral NeuroscienceQRviral proteaseGeneral Medicinebiochemical phenomena metabolism and nutritionbiology.organism_classificationViruspicornavirusViral proteaseCapsidMutationMedicineCapsid ProteinsHuman genomeDeep mutational scanningResearch ArticleHuman
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