scholarly journals On the nature of a glassy state of matter in a hydrated protein: Relation to protein function

2001 ◽  
Vol 98 (20) ◽  
pp. 11242-11247 ◽  
Author(s):  
M. M. Teeter ◽  
A. Yamano ◽  
B. Stec ◽  
U. Mohanty
Keyword(s):  
Protein Function ◽  
Glassy State ◽  
Hydrated Protein ◽  
State Of Matter

scholarly journals Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from Arabidopsis thaliana

Biomolecules ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 615
Author(s):  
Dirk K. Hincha ◽  
Ellen Zuther ◽  
Antoaneta V. Popova
Keyword(s):  
Protein Function ◽  
Glassy State ◽  
Detailed Knowledge ◽  
Lea Proteins ◽  
Cellular Survival ◽  
Intrinsically Disordered ◽  
Similar Information ◽  
Underlying Mechanisms ◽  
Sugar Glasses

Cells of many organisms and organs can withstand an (almost) total water loss (anhydrobiosis). Sugars play an essential role in desiccation tolerance due to their glass formation ability during dehydration. In addition, intrinsically disordered LEA proteins contribute to cellular survival under such conditions. One possible mechanism of LEA protein function is the stabilization of sugar glasses. However, little is known about the underlying mechanisms. Here we used FTIR spectroscopy to investigate sucrose (Suc) glass stability dried from water or from two buffer components in the presence of four recombinant LEA and globular reference proteins. Buffer ions influenced the strength of the Suc glass in the order Suc < Suc/Tris < Suc/NaP. LEA proteins strengthened the sugar H-bonded network and the molecular structure in the glassy state. The position of νOH peak and the wavenumber–temperature coefficient (WTCg) provided similar information about the H-bonded network. Protein aggregation of LEA proteins was reduced in the desiccation-induced Suc glassy state. Detailed knowledge about the role of LEA proteins in the stabilization of dry sugar glasses yields information about their role in anhydrobiosis. This may open the possibility to use such proteins in biotechnical applications requiring dry storage of biologicals such as proteins, cells or tissues.

scholarly journals Active topological glass

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Jan Smrek ◽  
Iurii Chubak ◽  
Christos N. Likos ◽  
Kurt Kremer
Keyword(s):  
Glass Transition ◽  
Soft Matter ◽  
Glassy State ◽  
Relaxation Times ◽  
Packing Fraction ◽  
Higher Eukaryotes ◽  
State Of Matter

AbstractThe glass transition in soft matter systems is generally triggered by an increase in packing fraction or a decrease in temperature. It has been conjectured that the internal topology of the constituent particles, such as polymers, can cause glassiness too. However, the conjecture relies on immobilizing a fraction of the particles and is therefore difficult to fulfill experimentally. Here we show that in dense solutions of circular polymers containing (active) segments of increased mobility, the interplay of the activity and the topology of the polymers generates an unprecedented glassy state of matter. The active isotropic driving enhances mutual ring threading to the extent that the rings can relax only in a cooperative way, which dramatically increases relaxation times. Moreover, the observed phenomena feature similarities with the conformation and dynamics of the DNA fibre in living nuclei of higher eukaryotes.

The glassy state of matter

1956 ◽  
Vol 13 (4) ◽  
pp. 171-173
Author(s):  
R. L. Myuller
Keyword(s):  
Glassy State ◽  
State Of Matter

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

2020 ◽  
Vol 477 (7) ◽  
pp. 1219-1225 ◽  
Author(s):  
Nikolai N. Sluchanko
Keyword(s):  
Protein Function ◽  
Intrinsically Disordered Protein ◽  
Structural Basis ◽  
Major Protein ◽  
Post Translational Modifications ◽  
Protein Protein Interaction ◽  
Intrinsically Disordered ◽  
Biochemical Journal ◽  
Multiple Binding ◽  
And Control

Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation. Phosphorylation can directly affect protein function and control recognition by proteins that ‘read’ the phosphorylation code, re-wiring the interactome. The eukaryotic 14-3-3 proteins recognizing multiple phosphoproteins nicely exemplify these concepts. Although recent studies established the biochemical and structural basis for the interaction of the 14-3-3 dimers with several phosphorylated clients, understanding their assembly with partners phosphorylated at multiple sites represents a challenge. Suboptimal sequence context around the phosphorylated residue may reduce binding affinity, resulting in quantitative differences for distinct phosphorylation sites, making hierarchy and priority in their binding rather uncertain. Recently, Stevers et al. [Biochemical Journal (2017) 474: 1273–1287] undertook a remarkable attempt to untangle the mechanism of 14-3-3 dimer binding to leucine-rich repeat kinase 2 (LRRK2) that contains multiple candidate 14-3-3-binding sites and is mutated in Parkinson's disease. By using the protein-peptide binding approach, the authors systematically analyzed affinities for a set of LRRK2 phosphopeptides, alone or in combination, to a 14-3-3 protein and determined crystal structures for 14-3-3 complexes with selected phosphopeptides. This study addresses a long-standing question in the 14-3-3 biology, unearthing a range of important details that are relevant for understanding binding mechanisms of other polyvalent proteins.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

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