BIOLOGICALLY IMPORTANT MACROMOLECULES PROTEINS. A very diverse group of macromolecules characterized...
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Transcript of BIOLOGICALLY IMPORTANT MACROMOLECULES PROTEINS. A very diverse group of macromolecules characterized...
![Page 1: BIOLOGICALLY IMPORTANT MACROMOLECULES PROTEINS. A very diverse group of macromolecules characterized by their functions: - Catalysts - Structural Support.](https://reader031.fdocuments.in/reader031/viewer/2022020320/5697bffa1a28abf838cc04b2/html5/thumbnails/1.jpg)
BIOLOGICALLY IMPORTANT MACROMOLECULESPROTEINS
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PROTEINS
A very diverse group of macromolecules characterized by their functions:- Catalysts- Structural Support- Transport Molecules (Ex: Transmembrane Proteins)- Movement of Muscles- Regulating Cellular Processes (Ex: Hormones)- Defense from Disease (Ex: Antibodies)
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PROTEINS
Monomer: Amino Acid
There are 20 different amino acids- R group/Side Chain changes for each
of the 20 amino acids
Polar due to the C=O, C-O, C-N and N-H
- R group also affects polarity
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PROTEINS
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PROTEINS
Amino acids can be joined by CONDENSATION/DEHYDRATION SYNTHESIS reactions to form dipeptides and polypeptides with PEPTIDE bonds (covalent bonds between the carboxyl and amino groups of adjacent amino acids)
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PROTEINS
The breakdown of a peptide bond involves the addition of a water molecule in a process known as HYROLYSIS
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PROTEINS
A protein made of 50 amino acids could have a possible 2050 different possible sequences
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PROTEIN ORGANIZATION
There are 4 different levels of protein organization:
PRIMARY STRUCTURE – the sequences of amino acids in a polypeptide strand
SECONDARY STRUCTURE – Since peptide bonds are polar, hydrogen bonding is possible between the C=O of one amino acid and the N-H of another. This results in either an alpha (α) helix or beta (β) sheet
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PROTEIN ORGANIZATION
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PROTEIN ORGANIZATION
TERTIARY STRUCTURE – the 3D folding of proteins as the peptide bonds and R groups interact with the aqueous environment (hydrophobic effect)- Hydrogen bonding between R groups and electrostatic
attractions between oppositely charged R groups- Assistance from molecular chaperones
QUATERNARY STRUCTURE – the clustering of two or more polypeptides in their tertiary structure
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PROTEIN ORGANIZATION
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PROTEIN DENATURATION
Protein completely unfolding when normal bonding between R groups is disturbed
Can be affected by extreme temperatures, changes in pH, exposure to chemicals, etc.
Proteins can no longer perform their usual function