dontmindme
Badges: 0
Rep:
? You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#1
Report Thread starter 7 years ago
#1
How does the 3D structure of proteins enable enzymes to perform their functions as biological catalysts?

I'm so confused!

I think it has something to do with their bonds but I'm not entirely sure. Does it involve the lock and key theory?
0
reply
Phoebe♥
Badges: 2
Rep:
? You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#2
Report 7 years ago
#2
Enzymes are proteins which have a tertiary (i think?) structure and this means that they have a complex shape, enabling substrates to be very specific to the enzyme (they have to have the shape which fits in)
0
reply
loperdoper
Badges: 15
Rep:
? You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#3
Report 7 years ago
#3
The lock and key theory involves the enzymes having a specific active site that is complementary to the substrate. The 3D structure will form the active site, allowing them to form the enzyme-substrate complex seen in the lock and key theory.

(Bonds within enzymes help form the tertiary structure, which is the 3D structure of the enzyme - so it does sort of have something to do with bonds, in a way)
0
reply
Dan12
Badges: 0
Rep:
? You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#4
Report 7 years ago
#4
(Original post by dontmindme)
How does the 3D structure of proteins enable enzymes to perform their functions as biological catalysts?

I'm so confused!

I think it has something to do with their bonds but I'm not entirely sure. Does it involve the lock and key theory?
Yes you're on the right track. The bonds in the tertiary structure determine an enzymes efficiency.

e.g. if the active site is positively charged (ionic bonds), +vely charged substrates would repel, where -vely charged substrates would be attracted.

similar approach with the other bonds associated with tertiary structure.
1
reply
dontmindme
Badges: 0
Rep:
? You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#5
Report Thread starter 7 years ago
#5
(Original post by Dan12)
Yes you're on the right track. The bonds in the tertiary structure determine an enzymes efficiency.

e.g. if the active site is positively charged (ionic bonds), +vely charged substrates would repel, where -vely charged substrates would be attracted.

similar approach with the other bonds associated with tertiary structure.
Thanks soo much! Sorry its late haha
0
reply
Kallisto
Badges: 22
Rep:
? You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#6
Report 7 years ago
#6
(Original post by dontmindme)
How does the 3D structure of proteins enable enzymes to perform their functions as biological catalysts?

I'm so confused!

I think it has something to do with their bonds but I'm not entirely sure. Does it involve the lock and key theory?
3D structure? do you mean the tertiary one of the proteins?

As you surely know, the different proteins emerge by different combinations of amino acids. These ones are bonding by the amino group of the one amino acid and the carboxyl group of the other one, when these amino acids are get into the charge state. After that a peptide bond hold these amino acids together. Another peptide bonds cause that more amino acids are bonding to a sequence, so a primary structure emerges.

These primary structures are bonding by ionic and hydrogen bonds to the secondary bonds, and the secondary bonds are bonding by disulfide bonds, at the end the tertiary structure was created.

According to what combinations of amino acids have existed in the primary stuctures before, the tertiary structure gets a certain function as biological catalyst.

I know there was an answer before, but I would explain you the background.
0
reply
dontmindme
Badges: 0
Rep:
? You'll earn badges for being active around the site. Rep gems come when your posts are rated by other community members.
#7
Report Thread starter 7 years ago
#7
(Original post by Kallisto)
3D structure? do you mean the tertiary one of the proteins?

As you surely know, the different proteins emerge by different combinations of amino acids. These ones are bonding by the amino group of the one amino acid and the carboxyl group of the other one, when these amino acids are get into the charge state. After that a peptide bond hold these amino acids together. Another peptide bonds cause that more amino acids are bonding to a sequence, so a primary structure emerges.

These primary structures are bonding by ionic and hydrogen bonds to the secondary bonds, and the secondary bonds are bonding by disulfide bonds, at the end the tertiary structure was created.

According to what combinations of amino acids have existed in the primary stuctures before, the tertiary structure gets a certain function as biological catalyst.

I know there was an answer before, but I would explain you the background.
Thanks, that more than explains the answer!
0
reply
X

Quick Reply

Attached files
Write a reply...
Reply
new posts
Back
to top
Latest

Do you know what you'll do if you don't get the grades you're hoping for?

Find something else in clearing (40)
28.99%
Take a gap year (22)
15.94%
Resit my exams (37)
26.81%
Look for alternate pathways to the career I want (18)
13.04%
I don't know yet (15)
10.87%
Something else (tell us in the thread) (6)
4.35%

Watched Threads

View All