An in silico study of how histone tail conformation affects the binding affinity of ING family proteins

Background Due to its intrinsically disordered nature, the histone tail is conformationally heterogenic. Therefore, it provides specific binding sites for different binding proteins or factors through reversible post-translational modifications (PTMs). For instance, experimental studies stated that...

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Bibliographic Details
Main Authors: Nadir Gül, Ahmet Yıldız
Format: Article
Language:English
Published: PeerJ Inc. 2022-09-01
Series:PeerJ
Subjects:
Online Access:https://peerj.com/articles/14029.pdf

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