1. Tyrosine - a structural glue for hierarchical protein assembly.
- Author
-
Maraldo A, Rnjak-Kovacina J, and Marquis C
- Subjects
- Intrinsically Disordered Proteins chemistry, Intrinsically Disordered Proteins metabolism, Humans, Proteins chemistry, Proteins metabolism, Phase Transition, Tyrosine chemistry, Tyrosine metabolism
- Abstract
Protein self-assembly, guided by the interplay of sequence- and environment-dependent liquid-liquid phase separation (LLPS), constitutes a fundamental process in the assembly of numerous intrinsically disordered proteins. Heuristic examination of these proteins has underscored the role of tyrosine residues, evident in their conservation and pivotal involvement in initiating LLPS and subsequent liquid-solid phase transitions (LSPT). The development of tyrosine-templated constructs, designed to mimic their natural counterparts, emerges as a promising strategy for creating adaptive, self-assembling systems with diverse applications. This review explores the central role of tyrosine in orchestrating protein self-assembly, delving into key interactions and examining its potential in innovative applications, including responsive biomaterials and bioengineering., Competing Interests: Declaration of interests The authors have no interests to declare., (Copyright © 2024 Elsevier Ltd. All rights reserved.)
- Published
- 2024
- Full Text
- View/download PDF