Related Experiment Video
Updated: Feb 12, 2026

A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model
Published on: November 25, 2022
Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities
Dipita Bhattacharyya1, Rakesh Kumar2, Surabhi Mehra2
1Department of Biophysics, Bose Institute, Kolkata 700 054, India. anirbanbhunia@gmail.com bhunia@jcbose.ac.in.
Abstract:
Familial mutations in α-synuclein affect the immediate chemical environment of the protein's backbone, changing its aggregation kinetics and forming diverse structural and functional intermediates. This study, concerning two oppositely aggregating mutants A30P and E46K, reveals a completely diverse conformational landscape for each, thus providing atomistic insights into differences in their aggregation dynamics.
Related Concept Videos
Protein Families
Protein Families
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Gene Families
Family Therapy
Strategic Family Therapy
Strategic family therapy emphasizes resolving communication barriers and improving problem-solving abilities...
Sources of Self-Esteem I: Family Experience

