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

Structural and folding dynamic properties of the T70N variant of human lysozyme.

The Journal of biological chemistry - 11 Jul 2003

Esposito Gennaro, Garcia Julian, Mangione Palma, Giorgetti Sofia, Corazza Alessandra, Viglino Paolo, Chiti Fabrizio, Andreola Alessia, Dumy Pascal, Booth David, Hawkins Philip N, Bellotti Vittorio

Abstract excerpt

Definition of the transition mechanism from the native globular protein into fibrillar polymer was greatly improved by the biochemical and biophysical studies carried out on the two amyloidogenic variants of human lysozyme, I56T and D67H. Here we report thermodynamic and kinetic data on folding as well as structural features of a naturally occurring variant of human lysozyme, T70N, which is present in the British...

Read the complete abstract on PubMed

Topics

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

Share to Ultraviolet Rays
Share to Amyloid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Amyloidosis

Share to Catalysis

Share to Circular Dichroism

Share to Guanidine

Share to Magnetic Resonance Spectroscopy

Share to Muramidase

Source

Identifiers

PMID: 12709420
DOI: 10.1074/jbc.M211000200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and folding dynamic properties of the T70N variant of human lysozyme.PMID 12709420Read ↗

Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.Semantic proximity Read ↗

Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.Semantic proximity Read ↗

Characterisation of the structural, dynamic and aggregation properties of the W64R amyloidogenic variant of human lysozyme.Semantic proximity Read ↗

Insights into the conformational changes of several human lysozyme variants associated with hereditary systemic amyloidosis.Semantic proximity Read ↗

Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy.Semantic proximity Read ↗

The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme.Semantic proximity Read ↗

Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.Semantic proximity Read ↗

Amyloid forming human lysozyme intermediates are stabilised by non-native amide-π interactionsSemantic proximity Read ↗

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.Semantic proximity Read ↗

The effects of mutation and modification on the structure and stability of human lysozyme: A molecular link between carbamylation and atherosclerosis.Semantic proximity Read ↗

A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation.Semantic proximity Read ↗

Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants.Semantic proximity Read ↗

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