High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid ?-peptide.
Related Articles High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid ?-peptide.
Chem Commun (Camb). 2018 May 01;54(36):4609-4612
Authors: Rosenman DJ, Clemente N, Ali M, García AE, Wang C
Abstract
Here we present the high pressure NMR characterization of A?42 and two A?40 variants with Alzheimer-causing mutations E22G and D23N. While chemical shifts only identified localized changes at ambient pressure compared with A?40, high pressure NMR revealed a common site with heightened pressure sensitivity at Q15, K16 and L17 in all three variants, which correlates to higher ?-propensity at central hydrophobic cluster (CHC) and faster aggregation.
PMID: 29670961 [PubMed - indexed for MEDLINE]
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