Showing posts with label Biochemistry. Show all posts
Showing posts with label Biochemistry. Show all posts

Sunday, May 1

Wednesday, September 8

I doubt...

In the name of Allah, the Most Beneficient, the Most Merciful.

Still remember we used to learn about trypthophan in our Biochemistry class? In case you don't remember, it is used to make serotonin, which turns into melatonin, the 'sleepy' hormone.

But, I've found out, from this book called The Care and Feeding of Your Brain by Kenneth Giuffer, pg 114, it says something different. I'll quote the whole thing.

"Chapter 5 - Sleep: Tracking the Source of Sound and Troubled Sleep

Booster and Zappers in Foods

...

Myth: Protein

Protein-laden food contain certain amino acids that have inherent stimulant properties. All meats can keep you awake because of their high protein content.
It is a myth that meats (such as turkey) high in trypthophan make you sleepy. Although they do contain sedative-like property, the amino acids in protien foods have stronger effect of wakefulness.

Myth: Warm milk

Sorry, but scientifically, your mother was wrong. Milk is high in protein, which makes it harder to fall asleep. However, the power of suggestion may overide this face. If you associate warm milk with home and warmth, and sound, secure sleep, the expectation of a good night's sleep following a glas of warm milk can make it happen."

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It is good to doubt. XD

Wednesday, August 11

Enzymology

In the name of Allah, the Most Beneficial, the most Merciful.

Uncompetitive inhibitors actually DECREASE the Michaelis-Menten constant. Have you ever wondered why?

According to what I've found from http://www.chm.davidson.edu/erstevens/Lineweaver/Lineweaver.html, the answer is this:

Uncompetitive inhibitors are thought to bind the E-S complex and not the enzyme. As with non-competitive inhibitors, the E-S-I complex cannot form the product. The product can only be formed from the E-S complex (Scheme 4). The effect of an uncompetitive inhibitor is to decrease both Vmax and Km. The drop in Km deserves some comment. Km is a measure of substrate affinity for the enzyme. A lower Km corresponds to a higher affinity. The presence of an uncompetitive inhibitor actually increases the affinity of the enzyme for the substrate. This surprising fact can be understood through the binding equilibrium. Since the inhibitor binds the E-S complex, the inhibitor decreases the concentration of the E-S complex. By Le Chatlier's principle, equilibrium of the enzyme and substrate will shift to form more E-S complex. Therefore, the enzyme demonstrates a higher affinity for the substrate eventhough this higher affinity does not lead to a higher Vmax. In a Lineweaver-Burk plot, uncompetitive inhibitors shift the line higher with a raised y-intercept.

Allah knows best.