Jasy19
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I'm reallllyy really stuck on a piece of merit and distinction work. I've made the connections of helixes to the structure, protecting and strengthening.. But I don't quite get this subject over all, and I don't know where to go from there. I've used collagen as an example of fibrous proteins, and I'm just at a standstill.

If anyone can help it'd be much appreciated
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Jasy19
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(Original post by Jasy19)
I'm reallllyy really stuck on a piece of merit and distinction work. I've made the connections of helixes to the structure, protecting and strengthening.. But I don't quite get this subject over all, and I don't know where to go from there. I've used collagen as an example of fibrous proteins, and I'm just at a standstill.

If anyone can help it'd be much appreciated

Doesn't have to neccessarily be collagen. I need to explain why a fibrous and globular protein are suited to their function, and how.
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Dynamo123
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(Original post by Jasy19)
Doesn't have to neccessarily be collagen. I need to explain why a fibrous and globular protein are suited to their function, and how.
Well, you can consider the function collagen has in the body. It acts as a very important component of extracellular matrix, it gives a sort of tensile strength to the structures like bone, in which it is present in the ECM. Now imagine what would happen if collagen became globular. Would it be able to perform its function of resisting shearing forces and imparting tensile strength? Would it be, in the form of reticular systems, able to interconnect different components of tissues? Boil it down to the basal lamina which separates epithelium from C.T. Will basal lamina remain functional if collagen is not fibrous.
Consider enzymes, for globular proteins. If the structure of enzymes is fibrous instead of globular, they can't perform their functions, because of the absence of specific domains for substrate binding in a fibrous structure.

I hope that helps.
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Jasy19
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Thank you very much, that's very helpful! Now to do some research on that and make sure I know the specifics
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Jasy19
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(Original post by Dynamo123)
Well, you can consider the function collagen has in the body. It acts as a very important component of extracellular matrix, it gives a sort of tensile strength to the structures like bone, in which it is present in the ECM. Now imagine what would happen if collagen became globular. Would it be able to perform its function of resisting shearing forces and imparting tensile strength? Would it be, in the form of reticular systems, able to interconnect different components of tissues? Boil it down to the basal lamina which separates epithelium from C.T. Will basal lamina remain functional if collagen is not fibrous.
Consider enzymes, for globular proteins. If the structure of enzymes is fibrous instead of globular, they can't perform their functions, because of the absence of specific domains for substrate binding in a fibrous structure.

I hope that helps.

In regards to the basal lamina, does C.T stand for connective tissue? And given epithelium is a certain type of connective tissue, is that what you mean? The seperation of two connective tissues within the extracellular matrix? Are there any specifics? It's all so hard to understand and research @[email protected]

What reasons are there for the solubility between the two? I know about amino acid chain polarities (hydrophillic/hydrophobic ends) but I don't know how they come into play with both globular and fibrous. I've got some stuff about integration within membrances, as well as active sites within enzymes, such as the channels created through polar acids protruding outwards from the membrane.

I thought the hydrophillic/phobic ends came about through the tertiary protein structure also?
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Dynamo123
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(Original post by Jasy19)
In regards to the basal lamina, does C.T stand for connective tissue? And given epithelium is a certain type of connective tissue, is that what you mean? The seperation of two connective tissues within the extracellular matrix? Are there any specifics? It's all so hard to understand and research @[email protected]

What reasons are there for the solubility between the two? I know about amino acid chain polarities (hydrophillic/hydrophobic ends) but I don't know how they come into play with both globular and fibrous. I've got some stuff about integration within membrances, as well as active sites within enzymes, such as the channels created through polar acids protruding outwards from the membrane.

I thought the hydrophillic/phobic ends came about through the tertiary protein structure also?
Yes, C.T. is connective tissue. Also, epithelium is not histologically a type of connective tissue. Epithelium is a separate class of tissue. There are four (according to others five) basic types of tissue, including muscle tissue, nerve tissue, epithelial tissue and C.T. And epithelium is not vascularized (supplied by blood vessels), while C.T. is. They are separated by a basal lamina through which nutrients diffuse from C.T. to epithelium. You can research it pretty well from some good book on histology, like Wheater's or Junqueira's.

Amino acids have a side chain R, due to which they might be hydrophobic, hydrophilic, polar, non-polar and a lot more else. These properties depend on the nature of the R chain, as you will get to know even more in University level Biochemistry. In an aqueous medium, the hydrophobic chains tend to cluster inside, while the hydrophilic chains tend to be attracted towards the water. This property is made use of in many different cases, including signalling by various molecules, as you will get to study later on.
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