AMINO ACIDS Flashcards
general formula for amino acids
amino group - c (with side chain sa baba) - carboxylic acid
NH - C - COOH
most ABUNDANT & FUNCTIONALLY DIVERSE molecules in living systems
PROTEINS
it is a LARGE MOLECULE that contains carbon, hydrogen, oxygen, & nitrogen (CHON)
PROTEINS
the chiral carbon is also called as
α - carbon (alpha carbon)
has 4 different groups attached to it
CHIRAL CENTER
what forms a peptide bond in amino acids
AMINO GROUP & CARBOXYLIC ACID GROUP
NH & COOH
proteins are
POLYPEPTIDE
every function in the living cells are HIGHLY DEPENDENT on
PROTEINS
a specialized protein of FLAGELLA is called
FLAGELLIN
an example of GLOBULAR PROTEIN
HEMOGLOBIN
component of hemoglobin that is RESPONSIBLE FOR THE PIGMENT or the red color of our blood
HEME
hemoglobin is a
TETRAMERIC
sides / groups of hemoglobin
2 - α
2- β
a special nucleus found in hemoglobin is known as
PROTOPHORPYRIN
turn genes ON & OFF to guide the differentiation of the cell and its later responsiveness to signals reaching it
TRANSCRIPTION FACTORS
the PRIMARY FUNCTION of protein is to provide the needed amino acids for maintaining an
ANABOLIC STATE
proteins play a vital role in the ________ system
NEURO-ENDOCRINE
one of the by product of protein metabolism
UREA
how many amino acids are involved in TRANSLATION
20
protein synthesis
TRANSLATION
how many amino acids are PRODUCED BY HUMANS?
AT LEAST 10
saan manggagaling ung another 10 amino acids that our body cannot produce
they must be supplemented in our diet
the other 10 amino acids that our body CANNOT PRODUCE is referred to as
ESSENTIAL AMINO ACIDS
what type of amino acids are produced by humans
L - α
what type of amino acids are produced by microorganisms
D amino acids
predominant amino acid in BACILLUS SUBTILIS
D-METHIONINE
Bacitracin & Gramicidin A
ANTIBIOTICS
Bleomycin
ANTITUMOR AGENT
Microcystin & Nodularin
CYANOBACTERIAL PEPTIDES
metabolic product of bacillus subtilis
BACITRACIN
has TYROCIDIN
GRAMICIDIN A
common side effect of BLEOMYCIN
pulmonary fibrosis
toxic microbial peptides
CYANOBACTERIAL PEPTIDES
an IMINO ACID
PROLINE
all amino acids posses the same functional group except
PROLINE
formed by the COOH of an amino acid and the NH₂ of the next amino acid
PEPTIDE BOND
peptide bonds has the capability to rotate because of this characteristic
PARTIAL DOUBLE BOND
the protation of peptide bonds are termed as
RESONANCE
forms a typical peptide group
RESONANCE
uncharged, single-bonded form is typically
60%
charged, double-bonded form is typically
40%
the peptide bond is an __ bond
AMINE BOND
these are very STABLE and NEUTRAL
AMIDES
amino acids are linked by
PEPTIDE BONDS
naming of peptides
drop -ine, palitan ng -yl
retained ang name ng terminal amino acid ( yung nasa dulo)
useful in classifying amino acids
R GROUP
the genetic code specifies how many amino acids
20
only what amino acids in human occurs in proteins
L - α amino acids
represents the vast majority of amino acids found in proteins
L-amino acids
found in some antibiotics and in the bacterial cell wall
D-amino acids
REACTIONS OF AMINO ACIDS
responsible for:
* acylation
* amidation
* esterification
AMINE GROUP
REACTIONS OF AMINO ACIDS
responsible for:
* esterification
* formation of amides and acid anhydrides
CARBOXYLIC ACID GROUP
the most important reaction of amno acids
PEPTIDE BOND FORMATION
- tend to interact with the aqueous environment, often involved in the formation of H-bonds
- predominnatly found on the exterior surfaces of proteins or in the reactive centers of enzymes
- Ser, Thr, Tyr
HYDROPHILIC AMINO ACIDS
- tend to repel the aqueous environment
- do not ionize or participate in the formation of H-bonds
- reside predominantly in the interior of proteins
- Ala, Val, Leu, Ile
HYDROPHOBIC AMINO ACIDS
allow enzyme reactions to occur
R GROUPS
act as either a proton donor or acceptor at physiological pH, thus play a important role in enzymatic catalysis
IMIDAZOLE RING og [H]
allow serine and threonine, cysteine to act as nucleophiles during enzymatic catalysis
primary alcohol of ser & thr
thiol of cys
____ of cysteine able to form a disulfide bonds with other cysteines
THIOL
____ of ser, tyr, and thr participate in the regulation of activity of enzymes
OH GROUP
amino aids may have positive, negative, or zero net charge
ZWITTERIONS
charge of zwitterion
both + & - charge
zwitterion is ____ overall
neutral
TESTS
- used to visualize spots or bands of amino acids separated by chromatography or electrophoresis
- deep purple color is formed with traces of any amino acid
- RUHEMANN’S PURPLE
REACTION W/ NINHYDRIN
TESTS
- General test for the presence of protein
- turns purple when mixed with a solution containing protein
- purple color is formed when copper ions in the reagent react with the peptide bonds of the polypeptide chains to form a complex
BIURET TEST
requirement of biuret test
should be polypeptide
kapag tripeptide, negative ang result
TESTS
- used to determine the presence of aromatic amino acids
- concentrated nitric acid will form a yellow complex with tryptophan and tyrosine side chains in proteins
XANTHOPROTEIC TEST
TESTS
test for tyrosine
MILLON’S TEST
TESTS
test for tryptophan
HOPKIN’S
TESTS
- disulfide bridges wil react with Pb²+ ion from lead acetate in an acidified solution
- a black precipitate (PbS) indicates the presence of disulfide bonded cysteine in proteins
LEAD ACETATE TEST