pH-dependent compaction of intrinsically disordered poly-E motif in titin

Manukian, Sophia; Punch, Emily; Gage, Matthew J.

doi:10.1016/j.bpj.2021.11.1752

Cited by 1 publication

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“…Ionization state changes are most apparent in very acidic or basic conditions, where dramatic structural changes may be evident ( Uversky, 2009 ). The PEVK repeats of titin exemplify this effect, as it shows a pH-dependent compaction of its structure ( Manukian et al, 2022 ). An IDR prediction tool named DispHred has been developed to characterize disorder propensity as a function of pH ( Santos et al, 2020 ).…”

Section: Myofilament-associated Protein With Intrinsic Disorder (Mapid)smentioning

confidence: 99%

Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling

Sun

Kekenes‐Huskey

2023

Quart. Rev. Biophys.

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The cardiac sarcomere is a cellular structure in the heart that enables muscle cells to contract. Dozens of proteins belong to the cardiac sarcomere, which work in tandem to generate force and adapt to demands on cardiac output. Intriguingly, the majority of these proteins have significant intrinsic disorder that contributes to their functions, yet the biophysics of these intrinsically disordered regions (IDRs) have been characterized in limited detail. In this review, we first enumerate these myofilament-associated proteins with intrinsic disorder (MAPIDs) and recent biophysical studies to characterize their IDRs. We secondly summarize the biophysics governing IDR properties and the state-of-the-art in computational tools toward MAPID identification and characterization of their conformation ensembles. We conclude with an overview of future computational approaches toward broadening the understanding of intrinsic disorder in the cardiac sarcomere.

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Section: Myofilament-associated Protein With Intrinsic Disorder (Mapid)smentioning

confidence: 99%