Proline periodicity modulates the self-assembly properties of elastin-like polypeptides.
Lisa D. Muiznieks,Fred W. Keeley +1 more
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TLDR
Investigation of the specific contribution of proline number and spacing to the structure and self-assembly propensities of elastin-like polypeptides supports a model where proline-poor regions of theElastin monomer provide a unique contribution to assembly and suggests a role for localized β-sheet in mediating self- assembly interactions.About:
This article is published in Journal of Biological Chemistry.The article was published on 2010-12-17 and is currently open access. It has received 66 citations till now. The article focuses on the topics: Tropoelastin & Elastin.read more
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Sequence heuristics to encode phase behaviour in intrinsically disordered protein polymers.
TL;DR: It is shown that intrinsically disordered, repeat proteins can be designed to exhibit tunable lower or upper critical solution temperature transitions in physiological solutions and that mutation of key residues at the repeat level abolishes phase behaviour or encodes an orthogonal transition.
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Molecular assembly and mechanical properties of the extracellular matrix: A fibrous protein perspective.
Lisa D. Muiznieks,Fred W. Keeley +1 more
TL;DR: An overview of the hierarchical molecular and supramolecular assembly of collagens and elastic fibers is provided, and their capacity for mechanical behavior in response to force is reviewed.
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Advances in Understanding Stimulus-Responsive Phase Behavior of Intrinsically Disordered Protein Polymers
TL;DR: The proposed framework and ongoing studies of stimulus-responsive phase behavior of designed IDPPs have direct implications in bioengineering, where designing sequences with bespoke material properties broadens the spectrum of applications, and in biology and medicine for understanding the sequence-specific driving forces for the formation of protein-based membraneless organelles.
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De novo engineering of intracellular condensates using artificial disordered proteins.
TL;DR: Artificial intrinsically disordered proteins (A-IDPs) have now been shown to form exclusionary, intracellular droplets that can be designed using simple principles that are based on the aromatic/aliphatic ratio and molecular weight.
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Tropoelastin: a versatile, bioactive assembly module
Steven G. Wise,Giselle C. Yeo,Matti A. Hiob,Jelena Rnjak-Kovacina,David L. Kaplan,Martin K.C. Ng,Anthony S. Weiss +6 more
TL;DR: Tropoelastin is compatible with synthetic and natural co-polymers, expanding the applications of its potential use beyond traditional elastin-rich tissues and facilitating finer control of biomaterial properties and the design of next-generation tailored bioactive materials.
References
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Journal ArticleDOI
Principles that Govern the Folding of Protein Chains
TL;DR: Anfinsen as discussed by the authors provided a sketch of the rich history of research that provided the foundation for his work on protein folding and the Thermodynamic Hypothesis, and outlined potential avenues of current and future scientific exploration.
Journal ArticleDOI
Protein Misfolding, Functional Amyloid, and Human Disease
TL;DR: The relative importance of the common main-chain and side-chain interactions in determining the propensities of proteins to aggregate is discussed and some of the evidence that the oligomeric fibril precursors are the primary origins of pathological behavior is described.
Journal ArticleDOI
Protein folding and misfolding
TL;DR: The manner in which a newly synthesized chain of amino acids transforms itself into a perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence and on multiple contributing influences from the crowded cellular milieu.
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The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure
TL;DR: This review critically assess the application of FTIR spectroscopy to the determination of protein structure by outlining the principles underlying protein secondary structure determination by FTIRSpectroscopy, and highlighting the situations in which FTIR Spectroscopy should be considered the technique of choice.
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Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
TL;DR: The results confirm the model of intermolecular β-sheet formation as a widespread underlying mechanism of protein aggregation and opens the door to a fully automated, sequence-based design strategy to improve the aggregation properties of proteins of scientific or industrial interest.