Amino Acids Flashcards
Building blocks of protein
Amino acids
Composed of alpha carbon
Amino acids
Unique to each amino acids
R (side chain)
Can act both as an acid and base
Amphoteric
Accepts hydrogen atom
Amino group
Donate hydrogen atom
Carboxyl group
Both positively and negatively charged amino acids
Zwitterion
Almost all amino acids
L-amino acids
Can be seen in cell walls / antiobiotics
D-amino acids
Connects amino acids to produce protein
Peptide bond
Used in protein synthesis
Magic 20 amino acids
Dependent on R chain
Chemical nature
Amino acids that synthesized by the body
Non-essential amino acids
Must be acquired thru diet
Essential amino acids
Synthesized in adequate amounts by adults, but supplemented in newborns
Semi-essential amino acids
Used to generate glucose thru gluconeogenesis
Glucogenic amino acids
Used to generate ketone bodies
Ketogenic amino acids
Used as an alternative energy source
Ketone bodies
Hydrophobic amino acids
Nonpolar and uncharged
Hydrophilic amino acids
Polar & uncharged
Are fundamental units of proteins
Amino acids
Simple molecules containing both a amine group and an acid group
Amino acids
Magic 20 is labeled by
Francis crick & James Watson
He determined the structure of DNA
Francis Crick & James Watson
This makes amino acids water-soluble
Zwitterion
It is protaned, giving the amino acid a positive charge
Carboxylate group
It is the pH at which an amino acid exists in its zwitterion form (equal amounts of protonated and deprotonated forms)
Isoelectric point
It is deprotonated, the amino acid giving a negative charge
Ammonium group
Molecules with a chiral carbon atom are optically active, meaning they can rotate plane polarized light
Chiral molecules
Only chiral amino acid, due to having two hydrogen atoms attached to the a-carbon
Glycine
Only forms found in proteins
L-amino acids
Found in some antibiotic and bacterial cell walls
D-amino acids
A way to represent the arrangement of groups around a chiral carbon atom
Fischer projection
These amino acids can hydrogen bond with water, making them more soluble than nonpolar amino acids
Polar and uncharged amino acids
A weaker acid than the primary carboxylic acid group in the Amino acid backbone
Secondary carboxylic acid group
It is important for interactions with metal ions, acting as nucleophiles in enzymes, and in ionic interactions
Side chain
It forms the guanidinium group
Arginine
It has a simple ammonium ion as its basic group
Lysine
Forms an imidazolium group
Histidine
These are found in collagen and gelatin
Hydroxylysine and hydroxyproline
Nonpolar side chains clump
together due to London dispersion
forces. They exclude water and
other side chains.
Hydrophobic interactions
Polar and uncharged side chains interact
through hydrogen bonding with
water and each other.
Hydrophilic interactions
Acidic and basic side chains with opposite
charges attract. A carboxylate
group from one side chain can form
an ionic bond with the ammonium
ion of another side chain.
Ionic interactions
Two cysteine molecules can form a disulfide
linkage through a mild oxidation
reaction.
Disulfide linkages
A protein is a chain of at least now many amino aids joined together
150
Is a crucial bond in biochemistry, formed between two amino acids through A dehydration reaction
Peptide bond
Product of two amino acids joined by peptide bond
Dipeptide
a flat, planar structure stabilized by resonance.
Peptide bond
formed by adding a third amino acid to a dipeptide.
Tripeptide
