This document explains in proteins in great detail, which may be simple but is a very complicated concept. The document includes class notes in black and syllabus notes in red. There are also links to past papers and practice questions. The SL and HL topics are both there. I recommend reading over ...
Biology ib SL and HL paper 1 and paper 2 review (with links and resources)
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Proteins ib biology introduction
Amino acids
• Amino acids contain an amino group, a carboxyl group, a carbon and a unique R group.
•
• Ribosomes condenses 2 amino acids into a dipeptide forming a peptide bond. This is called
anabolism.
• Peptide bonds are covalent bonds.
• Building monomers together builds a polymer.
• Hydrolysis breaks peptide bonds.
• All variable groups are always the same.
• Almost every protein is unique because there are infinite possibilities of polypeptides,
because they could be any length, the 20 amino acids could be in any order or combination.
• If a polypeptide contains just 7 amino acids there can be 20 to the power of 7 possible
polypeptides generated.
• Given that polypeptides can contain up to 30,000 amino acids, the different possible
combinations of polypeptides are effectively infinite.
• Genes are codes for making polypeptides.
• DNA is stored in the nucleus, yet the polypeptide is produced in the cytoplasm (by
ribosomes).
• MRNA is a message from the nucleus to ribosome- instruction for how to put the
polypeptide together.
• The genetic code is the sequence of bases on mRNA- this tells the ribosome which amino
acids to use.
• Mrna moves out of the nuclear pore.
• Some amino acids are polar or non polar, some are positively or negatively charged, some
contain Sulphur. These differences are found in the r group of the amino acids. The
properties of the amino acids determine how a polypeptide folds up into a protein.
• The order/sequence of the amino acids of which the protein is composed.
• Formed by covalent peptide bonds between adjacent amino acids.
• Controls all subsequent levels of structure.
• It looks like beads on a string.
•
Polypeptide secondary structure
• The chains of amino acids fold or turn upon themselves.
• Difference between secondary and primary structure: Held together by hydrogen bonds
between anime and carboxylic groups. Hydrogen bonds themselves are weak but when
there are many together it can be strong.
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