Key result
Engineered PEVK proteins from exons 161, 120, and 184 exhibited similar persistence lengths (0.92, 0.89, and 0.98 nm), indicating similar elastic properties regardless of proline content.
Population
Engineered PEVK proteins (polypeptides encoded by individual titin PEVK exons 161, 120, and 184)
Comparison
Measurement of persistence length using single… vs Comparison among polypeptides with varying…
Design
Preclinical
Authors
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PEVK exon diversity shapes titin elasticity; leaves open therapeutic targeting of passive stiffness in cardiomyopathy.
Individual titin PEVK exons encode polypeptides with similar elastic properties regardless of proline content, indicating that alternative splicing solely adjusts the length of the PEVK domain.
Sarkar et al. (2005) studied this question. Engineered PEVK proteins (exons 161, 120, and 184) was evaluated on Persistence length (p) of the engineered PEVK proteins. Engineered PEVK proteins from exons 161, 120, and 184 exhibited similar persistence lengths (0.92, 0.89, and 0.98 nm), indicating similar elastic properties regardless of proline content.