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Updated: Feb 11, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
High pressure NMR reveals conformational perturbations by disease-causing mutations in amyloid β-peptide
David J Rosenman1, Nicolina Clemente, Muhammad Ali
1Department of Biological Sciences, Rensselaer Polytechnic Institute, 110 Eighth Street, Troy, New York 12180, USA. wangc5@rpi.edu.
Abstract:
Here we present the high pressure NMR characterization of Aβ42 and two Aβ40 variants with Alzheimer-causing mutations E22G and D23N. While chemical shifts only identified localized changes at ambient pressure compared with Aβ40, high pressure NMR revealed a common site with heightened pressure sensitivity at Q15, K16 and L17 in all three variants, which correlates to higher β-propensity at central hydrophobic cluster (CHC) and faster aggregation.
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