AMINO ACIDS (20) Flashcards
- Aliphatic R group
- nonpolar
- non-essential
- Hydrophobic
- Ambivalent
- Neutral
- R group: Methyl group
ALANINE
[A]
Ala
ALIPHATIC AMINO ACIDS
they are also hydrophobic
VALINE
ISOLEUCINE
ALANINE
LEUCINE
GLYCINE
VIALG
- Aliphatic R group
- polar
- essential
- Basic
- R group: Guanidino group
ARGININE
[R]
Arg
- designed to BIND with PHOSPHATE
- important in NITROGEN METABOLISM
ARGININE
[R]
Arg
Test / Reaction for ARGININE
SAKAGUCHI TEST
amino acids with GUANIDINO GROUP
HISTIDINE
ARGININE
LYSINE
History ng Argentina is a Ly (lie)
- Aliphatic R group
- polar
- non essential
- Acidic
- R group: Carboxyl group
ASPARTIC ACID
[D]
Asp
one of the ACIDIC amino acid; acts as GENERAL ACIDS in ENZYME ACTIVE CENTERS
ASPARTIC ACID
[D]
Asp
- Aliphatic R group
- polar
- non essential
- R group: Amide group
ASPARAGINE
[N]
Asn
- amide of aspartic acid
- common site for attachment of CARBOHYDRATES IN GLYCOPROTEINS
ASPARAGINE
[N]
Asn
ACIDIC AMINO ACIDS
GLUTAMIC ACID
ASPARTIC ACID
GooD
- Aliphatic R group
- nonpolar
- non essential
- R group: Thiol group
CYSTEINE
[C]
Cys
- plays a key role in STABILIZING EXTRACELLULAR PROTEINS
- can react with ITSELF to form an oxidized dimer by formation of a DISULFIDE bond
CYSTEINE
[C]
Cys
SULFUR CONTAINING amino acids
CYSTEINE
METHIONINE
si ClassMate may Sulfur
- Aliphatic R group
- polar
- non essential
- R group: Carboxylic acid
GLUTAMIC ACID
[E]
Glu
- has one additonal CH₃
- interconvertible with α-ketoglutarate
- important in the BIOSYNTHESIS OF PROLINE
GLUTAMIC ACID
[E]
Glu
- Aliphatic R group
- nonpolar
- non essential
- R group: Hydrogen atom
GLYCINE
[G]
Gly
- SMALLEST amino acid
- ambivalent
- exists mainly as zwitterion
- together with porline, favors the formation of beta-turn/bends
- simplest
- low molecular wieght
- not chiral
GLYCINE
[G]
Gly
- Aromatic R group
- polar
- essential
- basic
- R group: Imidazole
HISTIDINE
[H]
His
- Aliphatic R group
- nonpolar
- essential
- R group: methyl group (sec butyl)
ISOLEUCINE
[I]
Ile
side chain is NOT REACTIVE and therefore NOT INVOLVED in any COVALENT CHEMISTRY in enzyme active centers
ISOLEUCINE
[I]
Ile
- Aliphatic R group
- nonpolar
- essential
- R group: Isobutyl
LEUCINE
[L]
Leu
- has one additional methylene group in its side chain compared with valine
- hydrophobic; buried in folded proteins
LEUCINE
[L]
Leu
- Aliphatic R group
- polar
- essential
- POSITIVELY CHARGED ɛ-amino group
- R group: amino group
LYSINE
[K]
Lys
- Aliphatic R group
- nonpolar
- essential
- R group: methylthioether
METHIONINE
[M]
Met
- has thiol ether
- plays role in metabolism forming SAM which act as METHYL DONOR during METHYLATION
METHIONINE
[M]
Met
- Aromatic R group
- nonpolar
- essential
- R group: Benzyl group
PHENYLALANINE
[F]
PhE
- derivative of alanine with a phenyl substituent on the β carbon
- hydrophobic
PHENYLALANINE
[F]
Phe
- Aliphatic R group
- nonpolar
- non essential
- R group: Pyrrol group
PROLINE
[P]
Pro
- an IMINO ACID
- when found in an α helix, the helix will have a slight bend due to the lack of the hydrogen bond
- found at the end of a helix or in turns or loops
PROLINE
[P]
Pro
- Aliphatic R group
- polar
- non essential
- R group: Hydroxymethyl group
SERINE
[S]
Ser
- differs from alanine in that one of the methylenic hydrogens is replaced by a hydroxyl group
- hydrophilic
SERINE
[S]
Ser
OH conatining amino acids
SERINE [S]
THREONINE [T]
TYROSINE [Y]
STY
- Aliphatic R group
- polar
- essential
- R group: hydroxyl group
THREONINE
[T]
Thr
- non aromatic OH
- α and β carbons are optically active
THREONINE
[T]
Thr
capable of rotating plane polarixed light either to the left or right
OPTICALLY ACTIVE
- Aromatic R group
- nonpolar
- essential
- R group: Indole ring
TRYPTOPHAN
[W]
Trp
amino acids with RING
HISTIDINE
TRYTOPHAN
TYROSINE
PHENYLALANINE
WHYP
- Aromatic R group
- polar
- nonessential
- R group: Phenolic
TYROSINE
[Y]
Tyr
is derived form phenylalanine by hydroxylation in the para position
TYROSINE
[Y]
Tyr
- Aliphatic R group
- nonpolar
- essential
- R group: Isopropyl group
VALINE
[V]
Val
hydrophobic, usually found in the interior of proteins
VALINE
[V]
Val
- does not bind or give off protons or participate in H or ionic bonds (alkyl groups, aromatic)
- side chain can be thought as “oily” or lipid like
- hydrophobic
NON POLAR AMINO ACIDS
- zero net charge at neutral pH
UNCHARGED POLAR amino acids
these can lose proton at alkaline pH
CYSTEINE [C]
TYROSINE [Y]
contain a polar OH- group that can participate in H-bond formation
SERINE [S]
THREONINE [T]
TYROSINE [Y]
contain a C=O group and an amide grup (both can participate in H-bond formation)
ASPARAGINE [N]
GLUTAMIC ACID [E]
POLAR amino acids should contain
Sulfur
Oxygen
Nitrogen
- proton donors
- fully ionized at neutral pH forming a negatively charged carboxylate group
ACIDIC amino acids
accepts protons
BASIC amino acids
are fully ionized and positvely charged amino acids
LYSINE [K]
ARGININE [R]
is weakly basic and the free amino acid is uncharged
HISTIDINE [H]
BASIC amino acids
HISTIDINE
ARGININE
LYSINE
ASPARAGINE
TRYTOPHAN
WHeRe Ka Na
ESSENTIAL AMINO ACIDS
Phenylalanine
Valine
Tryptophan
Threonine
Methionine
Histidine
Arginine
Leucine
Lysine
PVT. TIM HALL
- 21st amino acid
- Sec and U
- selenium atom replaces the S in its structural analog, cysteine
- it is inserted into polypeptides during translation
SELENOCYSTEINE
- produced by a specific tRNA and aminoacyl tRNA synthetase, it forms part of an unusual genetic code in these organisms, and is considered the 22nd proteinogenic amino acid
- Pyl and O
PYRROLYSINE
RARE AMINO ACIDS
found in collagen
4-hydroxyproline
5-hydroxylysine
RARE AMINO ACIDS
found in cell walls of bacteria
D-Glutamic acid
RARE AMINO ACIDS
found in earthworms
D-Serine
RARE AMINO ACIDS
a neurotransmitter
γ-aminobutyric acid
RARE AMINO ACIDS
constituent of the vitamin panthothenic acid
β-alanine
the only optically inactive amino acid
GLYCINE
