Reading...
Play button
Play button
Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
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?
|
Hydrogen
|
|
|
Which has a different setup than this?
|
Proline
|
|
|
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
|
|
|
Glycine
|
The smallest amino acid and has two hydrogen atoms with no side-chain
|
|
|
Alanine
|
Has a methyl group as side-chain
|
|
|
Valine
|
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?
|
Glycine
|
|
|
What is the largest amino acid?
|
Tryptophan
|
|
|
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?
|
Scurvy
|
|
|
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
|
|
|
|
|
