Modulation of human transthyretin stability by the mutations at histidine 88 studied by free energy simulation.

doi:10.1002/prot.26353

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

Back to search

Article

Modulation of human transthyretin stability by the mutations at histidine 88 studied by free energy simulation.

Proteins - 1 Nov 2022

Lee Kyung-Hoon, Kuczera Krzysztof

Abstract excerpt

Human transthyretin (TTR) is a homotetrameric plasma protein associated with a high percentage of β-sheet, which forms amyloid fibrils and accumulates in tissues or extracellular matrix to cause amyloid diseases. Free energy simulations based on all-atom molecular dynamics simulations were carried out to analyze the effects of the His88 → Arg, Phe, and Tyr mutations on the stability of human TTR. The calculated...

Topics

Histidine
Humans
Molecular Dynamics Simulation
Mutation
Prealbumin
Thermodynamics

Source

Open in PubMed

Identifiers

PMID: 35484710
DOI: 10.1002/prot.26353

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics