Zouhair et al 1993. 

chymotrypsin, created short linkers of His-Asp-Ser catalytic triad.

Replicated and found that the triad had same kinetic K's as chymotripsin and had same inhibition

Retracted paper.

TL;DR: Importance of 3-D structure in enzyme catalysis

Many different inhibators for treatment

Lots of different active site possibilities

HIV- Protease is a homo dimer

-found aspartic acid residue, now can design tipranivir

Anti- HIV drug.

alters shape of activase and Protease

cleaves hydrophobic target residue (aspartic acid)

physical differences: smaller than a normal elderly brain.

Peptide fragent from precursor protein A-Beta 43 residue (-I-A)

peptide prevention

change in 1 phenylalanine= fatal

a change in 1 AA can cause death

Causes folding errors = loss in >30% protein functioning

 loss of stability  = 75% monogenic disease

they don't always look how they are presented.

they fold and un-fold many times.

one state may be favored over another.

0 kcals

half folded and half un-folded

1. Geometry- partially planar polar bonds

2. Chemical nature of peptide bonds

Ala, A 

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Arg, R

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Asn, N

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Asp, D

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Cys, C

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gln, Q

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glu, E

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gln, Q

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His, H

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ile, I

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leu, L

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