SLE212 Study Guide - Final Guide: Enantiomer, Amine, Absorbance

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Amino Acids:
General Structure:
Chiral Carbon: Has 4 different groups attached.
Exception Glycine
Enantiomers: Mirror images of each other that are not super impossible
Occurs in nature: L
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Isoelectric Point: The pH point where the amino acid has no net charge.
Zwitterion: A molecule that has separate positive and negatively charged groups, giving it an overall
net charge of 0.
pKa: Tells us how acidic it is. The lower the pka the stronger the acid.
pH << pKa = Groups protonated (COO- COOH)
pH >> pKa = Groups deprotonated (COOH COO-)
Hydropathy: Ide of a aio aids hdrophoi/hdrophili properties of it’s side hai.
Important for determining protein folding!
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Classification of Amino Acids:
Hydrophobic: Non-polar side chains (Alkyl groups or aromatic rings)
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Document Summary

Enantiomers: mirror images of each other that are not super impossible. Isoelectric point: the ph point where the amino acid has no net charge. Zwitterion: a molecule that has separate positive and negatively charged groups, giving it an overall net charge of 0. pka: tells us how acidic it is. The lower the pka the stronger the acid: ph << pka = groups protonated (coo- cooh, ph >> pka = groups deprotonated (cooh coo-) Hydropathy: i(cid:374)de(cid:454) of a(cid:374) a(cid:373)i(cid:374)o a(cid:272)ids h(cid:455)dropho(cid:271)i(cid:272)/h(cid:455)drophili(cid:272) properties of it"s side (cid:272)hai(cid:374). Hydrophobic: non-polar side chains (alkyl groups or aromatic rings) Hydrophilic (neutral): polar side chains (oh or sh) Primary: linear polypeptide sequence: peptide (covalent) bonds. Secondary: folded version of polypeptide sequence stabilised by hydrogen bonds: hydrogen bonds. Domain: parts of a protein responsible for different functions. Peptide bond formation: h2o removed from a-carboxyl and an amino group. Amino residues: amino acids once incorporated into a protein or polypeptide.

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