Cold stability of intrinsically disordered proteins

Tantos, Ágnes; Friedrich, Péter; Tompa, Péter

doi:10.1016/j.febslet.2008.12.054

Cited by 51 publications

(46 citation statements)

References 38 publications

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“…All temperature effects were consistent with a decrease in structural propensity as expected for a more energetic ensemble of conformations, confirming that the ABM does not undergo cold denaturation [71]. Notably, the magnitude of the effect is two-fold stronger for the helical region (4-8 ppbÁK…”

Section: Discussionsupporting

confidence: 71%

New insights into the role of the disordered WIP N‐terminal domain revealed by NMR structural characterization

et al. 2015

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WASp-interacting protein (WIP) is an intrinsically disordered 503-residue polypeptide with a key role in actin polymerization in activated T cells. Its interaction with actin is mediated by a pair of conserved actin binding motifs (ABMs) at the WIP N-terminus, a domain that has not been investigated in its unbound form. Here we use NMR to investigate the biophysical behavior of the N-terminal ABM in WIP using protonless 13 C 0 -detected spectroscopy. Secondary chemical shifts, residual dipolar couplings and temperature effects identify residual structure throughout the ABM, which exhibits transient helical and b-strand character for residues 30-42 and 44-62, respectively. These observed structural propensities echo the structure observed in the actin-bound state of the ABM. Furthermore, residues preceding the canonical ABM (17-25) and conserved among WIP-related proteins exhibit transient b-strand character, suggesting that the WIP N interaction epitope extends towards the N-terminal polyproline motif. This suggests a possible role for this region in mediating the WIP interaction with polyproline binders such as profilin. In revealing these features of the WIP ABM this study demonstrates the unique ability of NMR in characterizing unstructured domains and provides necessary information for further investigation of WIP-mediated protein-protein interactions.

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Section: Discussionsupporting

confidence: 71%

New insights into the role of the disordered WIP N‐terminal domain revealed by NMR structural characterization

et al. 2015

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“…It has been reported that many kinds of dehydrins show cryoprotective activities. 30,[60][61][62][63][64][65][66][67] Considering that low temperature is a major environmental stress which promotes the expression of dehydrin genes, it could be concluded that the cryoprotection is a crucial function of dehydrins. Because the cryoprotective effect of ERD10 could not be enhanced by ATP, dehydrins do not seem to correspond to ATP-dependent cold stress chaperones.…”

Section: Binding To Macromoleculesmentioning

confidence: 99%

The multifunctionality of dehydrins: An overview

Hara¹

2010

Plant Signaling & Behavior

129

105

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Dehydrins are highly hydrophilic proteins that accumulate during embryogenesis and water stress responses in plants. Although dehydrins were discovered in the 1980s, their physiological functions are unknown. However, recent molecular-based studies have provided insights into the multifunctionality of dehydrins. The functional versatility of dehydrins is reviewed using recent experimental evidence, and perspectives in the functional studies of dehydrins are also discussed.for various purposes in the fields of agriculture, biotechnology, ecology and industry.

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“…Theoretically, cold denaturation should happen as a consequence of changes in the interactions between water and protein molecules at low temperatures and should represent a universal phenomenon. However, cold denaturation is difficult to study because most proteins have denaturation points below 0 • C [10]. Furthermore, the denaturation of protein during freezing could also occur as a consequence of changes in the solute concentration due to ice formation, exposure of protein to the ice-liquid interface and changes of the pH value surrounding the protein [11].…”

Section: Introductionmentioning

confidence: 99%