View source for 7pgd


==PAF in 50 v/v % DMSO-water solution==
<StructureSection load='7pgd' size='340' side='right'caption='[[7pgd]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pgd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_rubens_Wisconsin_54-1255 Penicillium rubens Wisconsin 54-1255]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PGD FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7pgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pgd OCA], [https://pdbe.org/7pgd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pgd RCSB], [https://www.ebi.ac.uk/pdbsum/7pgd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pgd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B6HWK0_PENRW B6HWK0_PENRW] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PAF and related antifungal proteins are promising antimicrobial agents. They have highly stable folds around room temperature due to the presence of 3-4 disulfide bonds. However, unfolded states persist and contribute to the thermal equilibrium in aqueous solution, and low-populated states might influence their biological impact. To explore such equilibria during dimethyl sulfoxide (DMSO)-induced chemical unfolding, we studied PAF and its inactive variant PAF(D19S) using nuclear magnetic resonance (NMR) and differential scanning calorimetry (DSC). According to the NMR monitoring at 310 K, the folded structures disappear above 80 v/v% DMSO concentration, while the unfolding is completely reversible. Evaluation of a few resolved peaks from viscosity-compensated (15)N-(1)H HSQC spectra of PAF yielded âG = 23 +/- 7 kJ/M as the average value for NMR unfolding enthalpy. The NMR-based structures of PAF and the mutant in 50 v/v% DMSO/H(2)O mixtures were more similar in the mixed solvents then they were in water. The (15)N NMR relaxation dynamics in the same mixtures verified the rigid backbones of the NMR-visible fractions of the proteins; still, enhanced dynamics around the termini and some loops were observed. DSC monitoring of the T(m) melting point showed parabolic dependence on the DMSO molar fraction and suggested that PAF is more stable than the inactive PAF(D19S). The DSC experiments were irreversible due to the applied broad temperature range, but still suggestive of the endothermic unfolding of PAF.

DMSO-Induced Unfolding of the Antifungal Disulfide Protein PAF and Its Inactive Variant: A Combined NMR and DSC Study.,Czajlik A, Batta A, Kerner K, Fizil A, Hajdu D, Raics M, Kover KE, Batta G Int J Mol Sci. 2023 Jan 7;24(2):1208. doi: 10.3390/ijms24021208. PMID:36674720<ref>PMID:36674720</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pgd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Penicillium rubens Wisconsin 54-1255]]
[[Category: Batta G]]
[[Category: Czajlik A]]