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

The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences.

Protein and peptide letters - 1 Jan 2023

Mizuno Fuko, Aoki Saeko, Matsugami Akimasa, Hayashi Fumiaki, Nishimura Chiaki

Abstract excerpt

INTRODUCTION: Sensitive methods are necessary to identify the residual structure in an unfolded protein, which may be similar to the functionally native structure. Signal intensity in NMR experiments is useful for analyzing the line width for a dynamic structure; however, another contribution is contained. METHODS: Here, the signal-intensity difference along the sequence was used for probability to calculate 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 Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 36600624
DOI: 10.2174/0929866530666230104140830
PMCID: PMC10230605

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences.PMID 36600624Read ↗

Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.Semantic proximity Read ↗

Residual Structure, Backbone Dynamics, and Interactions within the Synuclein FamilySemantic proximity Read ↗

A relationship between the aggregation rates of α-synuclein variants and the β-sheet populations in their monomeric forms.Semantic proximity Read ↗

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

Familial mutants of alpha-synuclein with increased neurotoxicity have a destabilized conformation.Semantic proximity Read ↗

Mutant protein A30P α-synuclein adopts wild-type fibril structure, despite slower fibrillation kinetics.Semantic proximity Read ↗

Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.Semantic proximity Read ↗

Protein-Protein Connections-Oligomer, Amyloid and Protein Complex-By Wide Line 1H NMR.Semantic proximity Read ↗

Conserved core of amyloid fibrils of wild type and A30P mutant α-synuclein.Semantic proximity Read ↗

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

<i>In vitro</i> -prepared A30P alpha-synuclein fibrils adopt the conserved and disease-relevant Greek key foldSemantic proximity Read ↗

In Vitro-Prepared A30P Alpha-Synuclein Fibrils Adopt the Conserved and Disease-Relevant Greek Key Fold.Semantic proximity Read ↗

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