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UID:1022@biotech.technion.ac.il
DTSTART;TZID=Asia/Jerusalem:20210413T150000
DTEND;TZID=Asia/Jerusalem:20220202T164952
DTSTAMP:20220512T124719Z
URL:https://biotech.technion.ac.il/events/biomolecular-recognition-protein
 -evolution/
SUMMARY:Biomolecular Recognition & Protein Evolution
DESCRIPTION:Biomolecular recognition is fundamental to the cellular functio
 ns via the formation of binding complexes. Functional complex of biomolecu
 lar recognition normally has high affinity and specificity which are shape
 d by the evolution. The affinity determines the stability of the complex w
 hile the specificity determines the discrimination of native complex again
 st competitive ones. The affinity can be quantified computationally and ex
 perimentally. However\, the specificity is challenging to be quantified si
 nce the comparison of all possible binding partners for the target biomole
 cule is a daunting task.\n\nBiological activities are mostly performed by 
 the proteins at the molecular scale. Naturally occurring proteins have a h
 igh degree of features different from random mixer of amino acids. They ha
 ve evolved to be able to spontaneously folding into native structure and s
 pecifically bind with their partners for functions. Darwin’s Theory of E
 volution suggests that natural selection imposes on the individuals and th
 e fittest survives. A fundamental question is how nature shapes the protei
 n interaction patterns for stable structure and specific functional bindin
 g at the molecular scale.\n\nIn this lecture\, I will introduce these two 
 topics (biomolecular recognition & protein evolution) and the attempt to a
 ddress the raised challenge and question with physical concept\, mathemati
 cal statistics and computational approaches. I will focus on the developme
 nt of the scoring function based on both the affinity and specificity opti
 mizations\, and the unification of physical principles for protein folding
 \, binding and evolution.
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