scholarly journals Drug and dye binding induced folding of the intrinsically disordered antimicrobial peptide CM15

RSC Advances ◽  
2017 ◽  
Vol 7 (65) ◽  
pp. 41091-41097 ◽  
Author(s):  
Ferenc Zsila ◽  
Szilvia Bősze ◽  
Kata Horváti ◽  
Imola Cs. Szigyártó ◽  
Tamás Beke-Somfai
Keyword(s):  
Antimicrobial Peptide ◽  
Conformational Transition ◽  
Drug Binding ◽  
Intrinsically Disordered ◽  
Induced Folding ◽  
Dye Binding ◽  
Natively Unfolded

Drug binding induces the disorder-to-order conformational transition of the natively unfolded antimicrobial peptide CM15.

Interactions of intrinsically disordered Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2 with membranes — synergistic effects of lipid composition and temperature on secondary structure

2010 ◽  
Vol 88 (5) ◽  
pp. 791-807 ◽  
Author(s):  
Luna N. Rahman ◽  
Lin Chen ◽  
Sumaiya Nazim ◽  
Vladimir V. Bamm ◽  
Mahmoud W. Yaish ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Synergistic Effects ◽  
Yukon Territory ◽  
Membrane Structures ◽  
Thellungiella Salsuginea ◽  
Intrinsically Disordered ◽  
Induced Folding ◽  
Large Unilamellar Vesicles ◽  
Unstructured Proteins ◽  
Extreme Cold

Dehydrins are intrinsically disordered (unstructured) proteins that are expressed in plants experiencing stressful conditions such as drought or low temperature. Dehydrins are typically found in the cytosol and nucleus, but also associate with chloroplasts, mitochondria, and the plasma membrane. Although their role is not completely understood, it has been suggested that they stabilize proteins or membrane structures during environmental stress, the latter association mediated by formation of amphipathic α-helices by conserved regions called the K-segments. Thellungiella salsuginea is a crucifer that thrives in the Canadian sub-Arctic (Yukon Territory) where it grows on saline-rich soils and experiences periods of both extreme cold and drought. We have cloned and expressed in Escherichia coli two dehydrins from this plant, denoted TsDHN-1 (acidic) and TsDHN-2 (basic). Here, we show using transmission-Fourier transform infrared (FTIR) spectroscopy that ordered secondary structure is induced and stabilized in these proteins by association with large unilamellar vesicles emulating the lipid compositions of plant plasma and organellar membranes. Moreover, this induced folding is enhanced at low temperatures, lending credence to the hypothesis that dehydrins stabilize plant outer and organellar membranes in conditions of cold.

scholarly journals The Mysterious Unfoldome: Structureless, Underappreciated, Yet Vital Part of Any Given Proteome

2010 ◽  
Vol 2010 ◽  
pp. 1-14 ◽  
Author(s):  
Vladimir N. Uversky
Keyword(s):  
Large Scale ◽  
Intrinsically Disordered Proteins ◽  
Biologically Active ◽  
Disordered Proteins ◽  
Unfolded Proteins ◽  
Intrinsically Disordered ◽  
Proteome Level ◽  
Natively Unfolded ◽  
Natively Unfolded Proteins

Contrarily to the general believe, many biologically active proteins lack stable tertiary and/or secondary structure under physiological conditions in vitro. These intrinsically disordered proteins (IDPs) are highly abundant in nature and many of them are associated with various human diseases. The functional repertoire of IDPs complements the functions of ordered proteins. Since IDPs constitute a significant portion of any given proteome, they can be combined in an unfoldome; which is a portion of the proteome including all IDPs (also known as natively unfolded proteins, therefore, unfoldome), and describing their functions, structures, interactions, evolution, and so forth. Amino acid sequence and compositions of IDPs are very different from those of ordered proteins, making possible reliable identification of IDPs at the proteome level by various computational means. Furthermore, IDPs possess a number of unique structural properties and are characterized by a peculiar conformational behavior, including their high stability against low pH and high temperature and their structural indifference toward the unfolding by strong denaturants. These peculiarities were shown to be useful for elaboration of the experimental techniques for the large-scale identification of IDPs in various organisms. Some of the computational and experimental tools for the unfoldome discovery are discussed in this review.

scholarly journals Calcium-Induced Folding and Stabilization of the Intrinsically Disordered RTX Domain of the CyaA Toxin

2010 ◽  
Vol 99 (11) ◽  
pp. 3744-3753 ◽  
Author(s):  
Alexandre Chenal ◽  
Johanna C. Karst ◽  
Ana Cristina Sotomayor Pérez ◽  
Anna Katarzyna Wozniak ◽  
Bruno Baron ◽  
...  
Keyword(s):  
Intrinsically Disordered ◽  
Induced Folding

scholarly journals DispHred: A Server to Predict pH-Dependent Order–Disorder Transitions in Intrinsically Disordered Proteins

2020 ◽  
Vol 21 (16) ◽  
pp. 5814 ◽  
Author(s):  
Jaime Santos ◽  
Valentín Iglesias ◽  
Carlos Pintado ◽  
Juan Santos-Suárez ◽  
Salvador Ventura
Keyword(s):  
Intrinsically Disordered Proteins ◽  
State Of The Art ◽  
Disordered Proteins ◽  
Protein Disorder ◽  
Net Charge ◽  
Intrinsically Disordered ◽  
Linear Boundary Condition ◽  
Natively Unfolded ◽  
Ph Dependent ◽  
Very High

The natively unfolded nature of intrinsically disordered proteins (IDPs) relies on several physicochemical principles, of which the balance between a low sequence hydrophobicity and a high net charge appears to be critical. Under this premise, it is well-known that disordered proteins populate a defined region of the charge–hydropathy (C–H) space and that a linear boundary condition is sufficient to distinguish between folded and disordered proteins, an approach widely applied for the prediction of protein disorder. Nevertheless, it is evident that the C–H relation of a protein is not unalterable but can be modulated by factors extrinsic to its sequence. Here, we applied a C–H-based analysis to develop a computational approach that evaluates sequence disorder as a function of pH, assuming that both protein net charge and hydrophobicity are dependent on pH solution. On that basis, we developed DispHred, the first pH-dependent predictor of protein disorder. Despite its simplicity, DispHred displays very high accuracy in identifying pH-induced order/disorder protein transitions. DispHred might be useful for diverse applications, from the analysis of conditionally disordered segments to the synthetic design of disorder tags for biotechnological applications. Importantly, since many disorder predictors use hydrophobicity as an input, the here developed framework can be implemented in other state-of-the-art algorithms.

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