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57 Cards in this Set

  • Front
  • Back
Overview of amino acid structure
All have the same chemical structure, with a carbon atom linked to an amino group, and a carboxyl group
What are amino acids distinguished by?
They are distinguished by a 3rd substituent
What is the fourth substituent?
Which has a different setup than this?
How is proline different?
The alpha carbon in proline and nitrogen contribute to a five member ring, with the other members of the ring being carbon
Proline is also the only _______ amino acid.
Secondary amino acid (or imino acid), due to the location of the amino group
Are the 3d structures of each amino acid imposable?
They exist as non-superimposable mirror images (or isomers)
What are the two special orientions?
L-amino and D-amino
How do proteins containing different configurations of amino acids interact with their environment differently?
They interact in different ways
How does this work?
Proteins recognize particular groups on asymmetric substrate molecules and bind differently
When do conformational problems result?
They result if both absolute configurations are allowed in a protein
What is a regular that prevents this?
An example are D-enzyme oxidases, which remove the wrong amino acids before they incorporated into proteins
What links neighboring amino acids?
Peptide bonds
What is a peptide bond?
It is the carboxyl group of one residue combining with the amino group, or the secondary amide of another
Written in sequence, the run from left to right with what on the left and what on the right?
Amino group on left, and Carbonyl group on the right, and Carbonyl group of the right
What are the aliphatic amino acids?
Glycine, Alanine, Valine, Leucine and Isoleucinene and Proline
Are aliphatic amino acids polar or nonpolar?
They are nonpolar
What are the uncharged polar amino acids?
Asparagine, Glutamine, Serine, Threonine
What are the sulfur containing amino acids
Methionine, Cysteine
What are the acidic amino acids?
Aspartic acid, Glutamic acid
What are the basic amino acids?
Arginine, Lysine, Histadine
The smallest amino acid and has two hydrogen atoms with no side-chain
Has a methyl group as side-chain
Branched chain
Do asparagine and glutamine side chains ionize?
No, but aspartic acid and glutamic acid to ionize
What do two cysteines come together to form between a disulfide bond?
They form a cystine
Is arginine a strong base or weak base?
It is a strong base because of the guanadino group
Histadine can have a positive charge on what?
Either of its two nitrogens (from having an imodozal side chain)
What is the smallest amino acid?
What is the largest amino acid?
What does the average amino acid weight?
About 110 daltons
So how can you find the number of amino acids in a polypeptdie chain?
Divide the weight by 110
What does SDS Gel do?
It separates proteins by size
What do nonpolar amino acids like to interact with, and how?
They like to interact with other nonpolar amino acids by hydrophobic interations
What do uncharged polar groups react with?
They react with one another
What do polar groups react with?
Charged groups
What do polar and charged polar groups react with to stabilize interactions between them?
They react with metal ions
What can uncharged polar residues form?
They can form nucleophiles
What are the charged polar residues?
Aspartic acid, glutamic acid, lysine, arginine, histidine, and cystine
What does proline hydroxylation do?
The addition of a hydroxide group in place of a hydroen turns the hydrophobic amino acid to uncharged polar
What is hydroxyproline abbundant in?
It is abundant in collagen, and gives strength to tissues through these hydrogen bonds between collagen molecules
What does prolal hydroxylase add to proline?
It adds a hydroxyl group to proline
This enzyme remains stable in active form by vitamin C, but a deficiency of it leads to what?
What does gamma carboxyglutamate do?
The side chain of glutamic acid is carboxylated, so then it has two carboxylg roups
Why is it called gamma carboxyglutamate?
It is called that because of the addition of carboxyl at the gamma carbon on the side chain
What does gamma carboxyglutamate react with?
It reacts with divalent cations like calcium
Where is it found?
It is found in regions of injury of the lipid bilayer, where calcium spills out of the membrane
The calcium reacts with regions of blood clotting protein leading to what?
Formation of a blood clot
What does a disease leading to a deficiency of gamma carboxyglutamate mean?
It means a deficiency of blood clots
What does phosphoserine do?
A hydrogen is substituted through phosphorylation by a phosphate in serine
What does this do functionally?
It acts in numerous processes including signalling cascade, hormone action mechanisms
What are two other residues with hydroxyl groups that can be phosphorylated?
Threonine and tyrosine
What do glycosylations do?
A single sugar chain of sugars are added to the side chain of amino acids location on specific protein
How does this impact cellular function?
Carbohydrates determine correct movement of proteins to correct cellular compartments in the cell
Gene splicing does what?
It alters the RNA encoding the protein
Proteolytic clips do what?
They modify translation products to form an active product