0000000000389021

AUTHOR

Zoltán Gáspári

showing 2 related works from this author

Disentangling the complexity of low complexity proteins

2020

Abstract There are multiple definitions for low complexity regions (LCRs) in protein sequences, with all of them broadly considering LCRs as regions with fewer amino acid types compared to an average composition. Following this view, LCRs can also be defined as regions showing composition bias. In this critical review, we focus on the definition of sequence complexity of LCRs and their connection with structure. We present statistics and methodological approaches that measure low complexity (LC) and related sequence properties. Composition bias is often associated with LC and disorder, but repeats, while compositionally biased, might also induce ordered structures. We illustrate this dichot…

Protein ConformationComputer scienceReview ArticleComputational biologyMeasure (mathematics)Evolution MolecularLow complexity03 medical and health sciencesProtein DomainsAmino Acid Sequencestructure[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Databases ProteinMolecular Biology030304 developmental biologyStructure (mathematical logic)0303 health sciencesSequence[SCCO.NEUR]Cognitive science/Neurosciencecomposition bias030302 biochemistry & molecular biologyProteinsdisorderlow complexity regionsStructure and function[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]AlgorithmsInformation SystemsBriefings in Bioinformatics
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Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases

2017

AbstractParvulins or rotamases form a distinct group within peptidyl prolyl cis-trans isomerases. Their exact mode of action as well as the role of conserved residues in the family are still not unambiguously resolved. Using backbone S2 order parameters and NOEs as restraints, we have generated dynamic structural ensembles of three distinct parvulins, SaPrsA, TbPin1 and CsPinA. The resulting ensembles are in good agreement with the experimental data but reveal important differences between the three enzymes. The largest difference can be attributed to the extent of the opening of the substrate binding cleft, along which motional mode the three molecules occupy distinct regions. Comparison w…

0301 basic medicineFine-tuningentsyymitStaphylococcus aureusparvulinsProtein ConformationParvulinenzymesTrypanosoma brucei bruceibinding cleftIsomeraseisomerasesArticleWW domain03 medical and health sciencesHumansAmino Acid SequenceMode of actionta116Multidisciplinary030102 biochemistry & molecular biologybiologyChemistryDynamics (mechanics)ta1182Peptidylprolyl IsomeraseArchaeaNIMA-Interacting Peptidylprolyl Isomerase030104 developmental biologyOrder (biology)PIN1Biophysicsbiology.proteinProtein BindingScientific Reports
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