4dj5: Difference between revisions
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==Proteinase K by Langmuir-Blodgett Hanging Drop Method at 1.8A resolution for Unique Water Distribution== | ==Proteinase K by Langmuir-Blodgett Hanging Drop Method at 1.8A resolution for Unique Water Distribution== | ||
<StructureSection load='4dj5' size='340' side='right' caption='[[4dj5]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4dj5' size='340' side='right'caption='[[4dj5]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4dj5]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4dj5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DJ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DJ5 FirstGlance]. <br> | ||
</td></tr> | </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=4dj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dj5 OCA], [https://pdbe.org/4dj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dj5 RCSB], [https://www.ebi.ac.uk/pdbsum/4dj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dj5 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ]] Hydrolyzes keratin at aromatic and hydrophobic residues. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Proteinase|Proteinase]] | *[[Proteinase 3D structures|Proteinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Parengyodontium album]] | ||
[[Category: Belmonte | [[Category: Belmonte L]] | ||
[[Category: Nicolini | [[Category: Nicolini C]] | ||
[[Category: Pechkova | [[Category: Pechkova E]] | ||
[[Category: Sivozhelezov | [[Category: Sivozhelezov V]] | ||
Revision as of 11:20, 21 September 2022
Proteinase K by Langmuir-Blodgett Hanging Drop Method at 1.8A resolution for Unique Water DistributionProteinase K by Langmuir-Blodgett Hanging Drop Method at 1.8A resolution for Unique Water Distribution
Structural highlights
Function[PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues. Publication Abstract from PubMedLangmuir-Blodgett films when used as nanotemplates for crystallization often leads to marked changes in protein stability and structure. Earlier we found that stability of proteins is also correlated with aqueous surroundings in the crystals. Here we study the direct relationships between presence of LB nanotemplates and unique patterns of water molecules surrounding the protein, for four model proteins for which 3D structures are available, and where crystallization conditions for each protein are the same except the presence of LB nanotemplate. Shape of frequency distribution of volumes occupied by water molecules were analyzed. They were found to be different between "classical" samples of different proteins, but surprisingly quite similar for LB samples. Volumes occupied by each water molecule as the function of the distance of the given molecule from the protein surface were studied. Introduction of LB film leads to appearance of water molecules close to protein surface but occupying large volumes. These findings confirm earlier experimental findings on the role of water molecules in determining protein stability and thereby pointing to water as a possible candidate for differences apparent in LB crystal stability against radiation. Unique water distribution of Langmuir-Blodgett versus classical crystals.,Pechkova E, Sivozhelezov V, Belmonte L, Nicolini C J Struct Biol. 2012 Jun 15. PMID:22706161[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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