Tubulin E-hook Hexamers Reveal Charge Dependent Compaction and Transient Secondary Structure Signatures
Bromley, A. C.; Kruse, N. A.; Brower, C. R.; Beam, M. K.; Hammer, N. I.; Fortenberry, R. C.; Reinemann, D. N.
Show abstract
This present work shows that E-hook fragments possess functional structure differences governed by electrostatic interactions and sequence composition. The acidic C-terminal tails of tubulin, known as E-hooks, play a central role in regulating interactions between microtubules and motor proteins, microtubule-associated proteins, and enzymatic modifiers. Despite their functional importance, the intrinsic structural properties of these peptide segments remain poorly characterized due to their intrinsically disordered nature. In this work, we present quantum-mechanically optimized structures of hexamer peptides derived from {beta}-tubulin E-hook sequences. Density functional theory calculations were used to optimize peptide geometries using progressively larger basis sets. From the optimized geometries we calculated theoretical Raman spectra, Ramachandran backbone dihedral distributions, and measured radii of gyration to resolve composition dependent structural tendencies. The combined Raman and conformational analyses provide a systematic computational approach for comparing simulated and experimental Raman spectra of tubulin E-hooks and other intrinsically disordered proteins and offer insight into how E-hooks contribute to the recognition mechanisms underlying the tubulin code.
Matching journals
The top 6 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Helix formation during the coupled binding and folding of intrinsically disordered proteins monitored by synchrotron-radiation circular dichroism spectroscopy 94%
- Folding and knotting of biotic and pre-biotic amino acid sequences through reverse evolution 94%
- Binding site plasticity regulation of the FimH catch-bond mechanism 94%
Similar papers in this journal
Similar papers in this journal
- Structural, Thermodynamic, and Dynamic Descriptors for Differential Mechanism of HIF-2 Activity Modulators 94%
- Covalent adducts formed by the androgen receptor transactivation domain and small molecule drugs remain disordered 93%
- PROTHON: A Local Order Parameter-Based Method for Efficient Comparison of Protein Ensembles 93%
Similar papers in this journal
- Oncogenic mutations in the DNA-binding domain of FOXO1 disrupt folding: quantitative insights from experiments and molecular simulations 93%
- A major disease-related point mutation in spastin alters dramatically the dynamics and allostery of the motor 93%
- Estimation of effective concentrations enforced by complex linker architectures using conformational ensembles. 92%
Similar papers in this journal
- Water inside the selectivity filter of a K+ ion channel: structural heterogeneity, picosecond dynamics, and hydrogen-bonding 94%
- Multiple Binding Configurations of Fis Protein Pairs on DNA: Facilitated Dissociation versus Cooperative Dissociation 93%
- Rational design of protein-specific folding modifiers 93%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.