Solvent accessibility of betaB2-crystallin and local structural changes due to deamidation at the dimer interface.

Experimental Eye Research
Takumi TakataKirsten J Lampi

Abstract

In the lens of the eye the ordered arrangement of the major proteins, the crystallins, contributes to lens transparency. Members of the beta/gamma-crystallin family share common beta-sheet rich domains and hydrophobic regions at the monomer-monomer or domain-domain interfaces. Disruption of these interfaces, due to post-translational modifications, such as deamidation, decreases the stability of the crystallins. Previous experiments have failed to define the structural changes associated with this decreased stability. Using hydrogen/deuterium exchange with mass spectrometry (HDMS), deamidation-induced local structural changes in betaB2-crystallin were identified. Deamidation was mimicked by replacing glutamines with glutamic acids at homologous residues 70 and 162 in the monomer-monomer interface of the betaB2-crystallin dimer. The exchange-in of deuterium was determined from 15 s to 24 h and the global and local changes in solvent accessibility were measured. In the wild type betaB2-crystallin (WT), only about 20% of the backbone amide hydrogen was exchanged, suggesting an overall low accessibility of betaB2-crystallin in solution. This is consistent with a tightly packed domain structure observed in the crystal structure. Deu...Continue Reading

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Citations

Mar 13, 2014·Progress in Biophysics and Molecular Biology·Kirsten J LampiLarry L David
May 5, 2012·Protein Expression and Purification·Ansgar Brock
Mar 13, 2014·Protein Science : a Publication of the Protein Society·Oksana A SergeevaKelly M Knee
Jul 21, 2015·Journal of Pharmaceutical and Biomedical Analysis·Takumi Takata, Noriko Fujii
Dec 3, 2014·Biochimica Et Biophysica Acta·Hiroaki SakaueNoriko Fujii
Jul 23, 2020·Protein Science : a Publication of the Protein Society·Calvin J VetterKirsten J Lampi
Dec 3, 2020·Structure·Alex J GusemanAngela M Gronenborn

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