Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Hydration Thermodynamics of Familial Parkinson's Disease-Linked Mutants of α-Synuclein.

Journal of chemical information and modeling - 26 Apr 2021

Aggarwal Leena, Biswas Parbati

Abstract excerpt

The hydration thermodynamics of different mutants of α-synuclein (α-syn) related to familial Parkinson's disease (PD) is explored using a computational approach that combines both molecular dynamics simulations in water and integral equation theory of molecular liquids. This analysis focuses on the change in conformational entropy, hydration free energy (HFE), and partial molar volume of α-syn upon mutation. The...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to alpha-Synuclein
Share to Entropy
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Parkinson Disease

Share to Thermodynamics

Source

Identifiers

PMID: 33749266
DOI: 10.1021/acs.jcim.1c00034

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Hydration Thermodynamics of Familial Parkinson's Disease-Linked Mutants of α-Synuclein.PMID 33749266Read ↗

Differentially heterogeneous hydration environment of the familial mutants of α-synuclein.Semantic proximity Read ↗

WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation.Semantic proximity Read ↗

Combined Effects of Mutation and Ionic Strength on α-Synuclein Reveal Generic Features of Aggregation-Prone Monomeric States.Semantic proximity Read ↗

Structures and Free Energy Landscapes of the Wild-Type and A30P Mutant-Type α-Synuclein Proteins with DynamicsSemantic proximity Read ↗

Comprehensive Structural and Thermodynamic Analysis of Prefibrillar WT α-Synuclein and Its G51D, E46K, and A53T Mutants by a Combination of Small-Angle X-ray Scattering and Variational Bayesian Weighting.Semantic proximity Read ↗

Synuclein Aggregation: Critical Role of Water in Entropy-Driven, Temperature-Responsive Aggregations of Macromolecules and CellsSemantic proximity Read ↗

Conformational Dynamics of α-Synuclein: A Study of its Intramolecular Forces in the Presence of Selected CompoundsSemantic proximity Read ↗

Post-translational modification sites are present in hydrophilic cavities of alpha-synuclein, tau, FUS, and TDP-43 fibrils: A molecular dynamics study.Semantic proximity Read ↗

Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.Semantic proximity Read ↗

Computational investigation on the effects of H50Q and G51D mutations on the α-Synuclein aggregation propensity.Semantic proximity Read ↗

Familial Parkinson Disease-associated Mutations Alter the Site-specific Microenvironment and Dynamics of α-SynucleinSemantic proximity Read ↗

Familial Mutations May Switch Conformational Preferences in α-Synuclein Fibrils.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.