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Article

NMR characterization of hydrophobic collapses in amyloidogenic unfolded states and their implications for amyloid formation.

Biochemical and biophysical research communications - 11 Jun 2010

Lim Kwang Hun, Nagchowdhuri Partha, Rathinavelan Thenmalarchelvi, Im Wonpil

Abstract excerpt

NMR spectroscopy was used to characterize hydrophobic clusters in amyloidogenic unfolded states of a protein and their implications for amyloid formation. Three local hydrophobic clusters were observed in the amyloidogenic state of the phosphatidylinositol 3-kinase (PI3K) SH3 domain. Our NMR studies showed that residues with high average area buried upon folding (AABUF) parameter collapsed to form the clusters....

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20438713
DOI: 10.1016/j.bbrc.2010.04.137

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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.

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