Search results for "Human proteins"

showing 3 items of 3 documents

Avoided motifs: short amino acid strings missing from protein datasets.

2020

Abstract According to the amino acid composition of natural proteins, it could be expected that all possible sequences of three or four amino acids will occur at least once in large protein datasets purely by chance. However, in some species or cellular context, specific short amino acid motifs are missing due to unknown reasons. We describe these as Avoided Motifs, short amino acid combinations missing from biological sequences. Here we identify 209 human and 154 bacterial Avoided Motifs of length four amino acids, and discuss their possible functionality according to their presence in other species. Furthermore, we determine two Avoided Motifs of length three amino acids in human proteins…

0301 basic medicinechemistry.chemical_classificationProtein functionAmino Acid Motifs030102 biochemistry & molecular biologyClinical BiochemistryComputational BiologyProteinsContext (language use)Computational biologyBiologyBiochemistryAmino acid03 medical and health sciences030104 developmental biologySecretory proteinchemistryAmino acid compositionCytoplasmMolecular BiologyHuman proteinsSequence AlignmentBiological chemistryReferences
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Between Interactions and Aggregates: The PolyQ Balance

2021

Abstract Polyglutamine regions (polyQ) are highly abundant consecutive runs of glutamine residues. They have been generally studied in relation to the so-called polyQ-associated diseases, characterized by protein aggregation caused by the expansion of the polyglutamine tract via a CAG-slippage mechanism. However, more than 4800 human proteins contain a polyQ, and only 9 of these regions are known to be associated with disease. Computational sequence studies and experimental structure determinations are completing a more interesting picture in which polyQ emerge as a motif for modulation of protein-protein interactions. But long polyQ regions may lead to an excess of interactions, and produc…

AcademicSubjects/SCI01140AcademicSubjects/SCI01130aggregationCAG-expansion diseasesContext (language use)Computational biologyReviewPolyglutamine tractBiologyProtein aggregationProtein–protein interactionhomorepeatprotein–protein interactionCodon usage biasGeneticsHumansPeptidesHuman proteinspolyglutamineEcology Evolution Behavior and SystematicsFunction (biology)Sequence (medicine)Genome Biology and Evolution
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Flanking regions determine the structure of the poly-glutamine homo- repeat in huntingtin through mechanisms common among glutamine-rich human protei…

2020

International audience; The causative agent of Huntington's disease, the poly-Q homo-repeat in the N-terminal region of huntingtin (httex1), is flanked by a 17-residue-long fragment (N17) and a proline-rich region (PRR), which promote and inhibit the aggregation propensity of the protein, respectively, by poorly understood mechanisms. Based on experimental data obtained from site-specifically labeled NMR samples, we derived an ensemble model of httex1 that identified both flanking regions as opposing poly-Q secondary structure promoters. While N17 triggers helicity through a promiscuous hydrogen bond network involving the side chains of the first glutamines in the poly-Q tract, the PRR prom…

Repetitive Sequences Amino AcidHuntingtinAmino Acid Motifs[SDV.BBM.BP] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biophysics03 medical and health sciencesHuntington's diseaseStructural BiologyHuman proteome projectmedicineHumans[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyHuman proteinsProtein secondary structure[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]030304 developmental biology[INFO.INFO-BI] Computer Science [cs]/Bioinformatics [q-bio.QM]Huntingtin Protein0303 health sciencesChemistry030302 biochemistry & molecular biologyPromotermedicine.diseaseCell biologyIntrinsically Disordered ProteinsGlutamine[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsPolyglutamic Acid[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Low Complexity Region
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