Article
Myopathy-associated G154S mutation causes important changes in the conformational stability, amyloidogenic properties, and chaperone-like activity of human αB-crystallin.
Biophysical chemistry - 1 Mar 2022
Khoshaman Kazem, Ghahramani Maryam, Shahsavani Mohammad Bagher, Moosavi-Movahedi Ali Akbar, Kurganov Boris I, Yousefi Reza
Abstract excerpt
Glycine to serine substitution at position 154 of human αB-crystallin (αB-Cry) is behind the development of cardiomyopathy and late-onset distal myopathy. The current study was conducted with the aim to investigate the structural and functional features of the G154S mutant αB-Cry using various spectroscopic techniques and microscopic analyses. The secondary and tertiary structures of human αB-Cry were preserved...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
