Comment on "Twisted Protein Aggregates and Disease: The Stability of Sickle Hemoglobin Fibers"
Y. Liu, J. D. Gunton

TL;DR
This paper revises the analysis of sickle hemoglobin fiber stability, emphasizing the role of elastic interactions in biopolymer aggregate formation using nucleation theory.
Contribution
It provides a corrected theoretical framework for understanding the stability of twisted protein fiber aggregates, specifically sickle hemoglobin fibers.
Findings
Elastic interactions influence fiber bundle radii.
Corrected nucleation theory offers new insights into fiber stability.
Implications for understanding sickle cell disease mechanisms.
Abstract
Aggregates of twisted protein fibers, such as sickle hemoglobin and actin, are important examples of biopolymers in which elastic interactions play a crucial role in determining the (metastable) bundle radii. Here, we present a corrected version of analysis on the stability of sickle hemoglobin fibers using the classic nucleation theory.
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Taxonomy
TopicsProtein Structure and Dynamics · Hemoglobin structure and function · Blood properties and coagulation
