Discriptions
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| Carboxylic acid side chains pka around 4 so they are unprotonated and negatively charged at physiologic pH Are hydrophilic and can form hydrogen and ionic bonds | Aspartate (aspartic acid)
and
Glutamate (glutamic acid)
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| All polar but not charged so H-bonding N residues in proteins are often glycosylated | Asparagine
Glutamine
Tryptophan
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| Side chain pKa's are 10-12 so they are positively charged at neutral pH Ionic and H bonding Significant hydrophobic portions in proteins the chains frequently are hiding in the interior with the positive ends sticking out at the surface | Arginine
Lysine
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| Have hyroxyl (OH) groups OH is a common site of postranslational modification (esp phosphorylation) Polar but not charged so H-bonds | Serine
Threonine
Tyrosine
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| Side chain has pKa of 6 so unprotonated at physio pH it is predominantly positively charged Can participate in H and ionic bonding Because it's side chain pKa is 6 it is a good buffer | Histidine
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| Side chain is easily oxidized and reduced, can form covalent bonds Disulfide bonds are very important for the structure of many proteins Cystine (two cysteins with a disulfide bridge) can form in blood- can form calculi | Cystein
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| Except for M the side chains have only C and H atoms Side chains aren't ionizable or polar so they are hydrophobic Degree of hydrophobicity varies V, L, and I are the "branched chain" amino acids (remember this) | Glycine
Alanine
Proline
Valine
Leucine
Isoleucine
Phenylalanine
Methionine
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Created by:
calebbaxter09
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