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August 25, 2025, 10:01:45 am

Author Topic: SAC 2  (Read 921 times)  Share 

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Em.

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SAC 2
« on: March 17, 2012, 04:59:01 pm »
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Hey everyone  :)
So I'm having my second sac for biology this coming Monday (19th) ... and my teacher didn't tell us much about it except for the fact that it will be on enzymes.
What should I focus on studying?
 Has everyone else done their second sac btw? ( I feel like we're behind - we're doing photosynthesis atm)...

ggxoxo

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Re: SAC 2
« Reply #1 on: March 17, 2012, 07:33:04 pm »
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If you did a prac, there probably would be lab qns lie what is the control, the independent and dependent variable

And then the general qns, like applying your knowledge to unknown contexts, definitions

saheh

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Re: SAC 2
« Reply #2 on: March 17, 2012, 08:21:36 pm »
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We have the same sac :) and we've just done photosynthesis too

We were told to know:
What effecives the rate of enzyme activity
How enzymes can be denatured
Lock&key and induced fit

Good luck!
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LOLs99

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Re: SAC 2
« Reply #3 on: March 17, 2012, 10:58:26 pm »
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More on graphs for enzymes.
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Em.

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Re: SAC 2
« Reply #4 on: March 18, 2012, 10:00:39 am »
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Thanks guys  :) hey do we have to memorize info about certain enzymes or nah?

LOLs99

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Re: SAC 2
« Reply #5 on: March 18, 2012, 02:41:57 pm »
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I suggest knowing a few...such as pepsin,trypsin...you gotta know these!(bottom)

Just describing how each factor actually affects enzyme activity:

*Heat - By adding heat, you overcome/break the weak intermolecular bonds (such as hydrophobic interactions and hydrogen bonding) that hold the shape of the secondary and tertiary structures in the enzyme, and hence the enzyme will denature and enzyme activity will sharply drop after the critical point (the temperature where enzymes begin to denature)
*pH - In order to maintain a constant level of pH, amino acids in the enzyme will donate or accept hydrogen ions, so that the pH level is stabilised. However, this changes the intermolecular bonds that form between the secondary and tertiary structures (as you've pretty much changed the chemical structure of the amino acid), and hence the protein will denature. The curve for pH affecting enzyme activity resembles a bell-curve because the pH scale is a logarithmic scale, which means that it goes up in factors of 10 (pH 6 is 10 times more acidic, and has 10x more hydrogen ions than pH 7), and so the drop in enzyme activity is not as dramatic as temperature.
*Co-enzymes - these basically help the enzyme to accommodate the substrate better, and make it easier to fit. Hence, enzyme activity will increase as more substrates will easily bind to the active site of the enzyme.
*Inhibitors - These are divided into two categories, non-competitive and competitive, which bind completely to an enzyme's active site, preventing the substrate from binding to the enzyme. If you have a high concentration of competitive inhibitors, enzyme activity will decrease as less substrate is able to bind to the active sites of enzymes. However, if the concentration of substrate is greater than the concentration of competitive inhibitors, enzyme activity will decrease less as the substrate becomes more 'competitive', and there is a lesser likelihood of an inhibitor binding to an active site. Non-competitive inhibitors almost permanently bind to enzymes, halting reactions between substrates and enzymes completely.
-Concentration of enzyme - Obviously, as you increase the concentrations of enzyme, there will be a great increase in the rate of reaction - more enzymes are bumping and binding into substrates.
-Concentration of substrate - Initially, increasing the substrate concentration will increase the rate of reaction as there is a greater chance of substrates binding to active sites, but it slowly decreases as the enzyme concentration becomes 'saturated', which is when the enzymes are reacting at full capacity and cannot increase the rate of reaction.

Hope that helps. :)
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