1l18
HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3
Template:ABSTRACT PUBMED 3405287
About this StructureAbout this Structure
1l18 is a 1 chain structure of Hen Egg-White (HEW) Lysozyme with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Matsumura M, Becktel WJ, Matthews BW. Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3. Nature. 1988 Aug 4;334(6181):406-10. PMID:3405287 doi:http://dx.doi.org/10.1038/334406a0
- ↑ Becker A, Kabsch W. X-ray structure of pyruvate formate-lyase in complex with pyruvate and CoA. How the enzyme uses the Cys-418 thiyl radical for pyruvate cleavage. J Biol Chem. 2002 Oct 18;277(42):40036-42. Epub 2002 Aug 5. PMID:12163496 doi:http://dx.doi.org/10.1074/jbc.M205821200