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WVSOM Amino Acids

Discriptions

QuestionAnswer
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)
All polar but not charged so H-bonding N residues in proteins are often glycosylated Asparagine Glutamine Tryptophan
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
Have hyroxyl (OH) groups OH is a common site of postranslational modification (esp phosphorylation) Polar but not charged so H-bonds Serine Threonine Tyrosine
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
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
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
Created by: calebbaxter09 on 2011-08-04



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