Lotem haleva/test page: Difference between revisions

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Trypsin contains an "oxyanion hole" formed by the backbone amide hydrogen atoms of <scene name='60/607865/Oxyanion_hole/1'>Gly-193 and Ser-195</scene> , which serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides.
Trypsin contains an "oxyanion hole" formed by the backbone amide hydrogen atoms of <scene name='60/607865/Oxyanion_hole/1'>Gly-193 and Ser-195</scene> , which serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides.
The  <scene name='60/607865/Asp_189/1'>aspartate residue</scene>  located in the catalytic pocket (S1) of trypsin is responsible for attracting and stabilizing positively charged lysine and/or arginine, and is, thus, responsible for the specificity of the enzyme.
The  <scene name='60/607865/Asp_189/1'>aspartate residue</scene>  located in the catalytic pocket (S1) of trypsin is responsible for attracting and stabilizing positively charged lysine and/or arginine, and is, thus, responsible for the specificity of the enzyme.
== Disease ==
== Mechanism ==


== Relevance ==
== Relevance ==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Lotem Haleva, Michal Harel