Structural highlights
Function
PRTK_PARAQ Hydrolyzes keratin at aromatic and hydrophobic residues.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A detailed analysis of structural and intensity changes induced by X-ray radiation is presented for two types of proteinase K crystals: crystal grown by classical hanging drop method and those grown by Langmuir-Blodgett (LB) nanotemplate. The comparison of various parameters (e.g. intensity per sigma ratio, unit-cell volume, number of unique reflections, B-factors) and electron density maps as a function of radiation dose, demonstrates that crystals, grown by the LB nanotemplate method, appear to be more resistant against radiation damage than crystals grown by the classical hanging drop method.
Radiation stability of proteinase K crystals grown by LB nanotemplate method.,Pechkova E, Tripathi S, Ravelli RB, McSweeney S, Nicolini C J Struct Biol. 2009 Dec;168(3):409-18. Epub 2009 Aug 15. PMID:19686853[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pechkova E, Tripathi S, Ravelli RB, McSweeney S, Nicolini C. Radiation stability of proteinase K crystals grown by LB nanotemplate method. J Struct Biol. 2009 Dec;168(3):409-18. Epub 2009 Aug 15. PMID:19686853 doi:10.1016/j.jsb.2009.08.005
