Search results for "Protein model"

showing 2 items of 2 documents

Sequence Determines Degree of Knottedness in a Coarse-Grained Protein Model

2015

Knots are abundant in globular homopolymers but rare in globular proteins. To shed new light on this long-standing conundrum, we study the influence of sequence on the formation of knots in proteins under native conditions within the framework of the hydrophobic-polar (HP) lattice protein model. By employing large scale Wang-Landau simulations combined with suitable Monte Carlo trial moves we show that, even though knots are still abundant on average, sequence introduces large variability in the degree of self-entanglements. Moreover, we are able to design sequences which are either almost always or almost never knotted. Our findings serve as proof of concept that the introduction of just o…

Protein ConformationFOS: Physical sciencesGeneral Physics and AstronomyCondensed Matter - Soft Condensed Matterstomatognathic systemComputer SimulationMathematicsSequence (medicine)chemistry.chemical_classificationQuantitative Biology::BiomoleculesDegree (graph theory)Proteinsfood and beveragesBiomolecules (q-bio.BM)Knot theoryAmino acidsurgical procedures operativeModels ChemicalQuantitative Biology - BiomoleculeschemistryFOS: Biological sciencesProtein modelSoft Condensed Matter (cond-mat.soft)Biological systemHydrophobic and Hydrophilic InteractionsMonte Carlo MethodPhysical Review Letters
researchProduct

Dynamic Structural Changes and Thermodynamics in Phase Separation Processes of an Intrinsically Disordered–Ordered Protein Model

2021

Elastin-like proteins (ELPs) are biologically important proteins and models for intrinsically disordered proteins (IDPs) and dynamic structural transitions associated with coacervates and liquid-liquid phase transitions. However, the conformational status below and above coacervation temperature and its role in the phase separation process is still elusive. Employing matrix least-squares global Boltzmann-fitting of the circular dichroism spectra of the ELPs (VPGVG) 20 , (VPGVG) 40 and (VPGVG) 60 , we found that coacervation occurs sharply when a certain number of repeat units has acquired β-turn conformation (in our sequence setting a threshold of ~20 repeat units). The differential scatter…

Models Molecular540 Chemistry and allied sciencesPhase transitionCircular dichroismCoacervateProtein ConformationChemistryPhase separation processCircular DichroismSequence (biology)General ChemistryIntrinsically disordered proteinsCircular dichroism spectraCatalysisIntrinsically Disordered Proteins540 ChemieBiophysicsProtein modelHumansThermodynamicsPeptidesAngewandte Chemie International Edition
researchProduct