 Lei Jin (source code)

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= Lei Jin
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<Lei Jin> coauthored structural research on how <heparin> activates the inhibitory <protein> <antithrombin>. A 1997 paper compared crystallographic structures involving active and latent <antithrombin> and its high-affinity five-sugar binding sequence at 2.9-ångström resolution.<The anticoagulant activation of antithrombin by heparin by Lei Jin and others>[Original byline and Abstract; pentasaccharide-associated structures]{ref}

The study linked binding to changes in the main <beta sheet> and exposure of the <reactive-center loop>, providing a structural account of how a carbohydrate ligand changes the behaviour of a <serpin>.<The anticoagulant activation of antithrombin by heparin by Lei Jin and others>[Abstract; conformational changes associated with activation]{ref} The point is more informative than simply observing that <heparin> and <antithrombin> bind: the locations of structural changes suggest how binding can alter access to the inhibitory machinery.

A structure is a constrained molecular snapshot. Establishing a complete time sequence or the rate of inhibition requires additional kinetic evidence; it cannot be read directly from a static arrangement of <atoms>.

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