BIOCHEM LAB_ QUIZ 1 Flashcards
Organic molecules that serve as the building blocks of proteins
Amino Acids
Short chains of amino acids
Peptides
Longer and complex peptides
Polypeptides
Structure of Amino Acids
Amino Group - left
Side chain or R group - bottom
Carboxyl group - right
Hydrogen - up
Alpha carbon - center
Proton or hydrogen donor
Acid
Proton acceptor / accepts hydrogen
Base
Molecule that contains both positive and negative charge
Zwitterion form
Negative charge in zwitterion form
Carboxylate ion
Positive charge in zwitterion form
Ammonium ion
Process of formation of peptides
Condensation
Happens when the reactive amino group of an amino acid interacts with the reactive carboxylic group of another amino acid
Condensation
Librates water molecules
Condensation
2 amino acids
Dipeptide
3 amino acids
Tripeptide
50 amino acids or more
Proteins or polypeptides
Aka amphoteric
Acid-base property
Act as a base and an acid depending on the reactant involved in the chemical reaction
Amphoteric
Acts as a base when an acid is added in the system
Amino acid
Acts an an acid when a base is added in the system
Amino acids
Results to overall charge of POSITIVE because?
Because of the reactive ammonium ion
Donates 1 hydrogen ion to the OH group from the base and becomes an _________ group
Amino
Donates 1 hydrogen ion to the OH group from the base
Ammonium ion
This results to an overall charge of NEGATIVE because?
Coming from the carboxylate
There is a certain pH where is EVENLY BALANCED between 2 forms
Isoelectric point
As the dipolar zwitterion with a net charge of ________
Zero
There is a negative and a positive pole
Dipolar
As the pH moves away from the isoelectric point, the amino acids may exist as __________ or an __________.
Cations and ion
As the pH become lower than the isoelectric point, it happens when acids is added in the system. The amino acids become _______ charge.
positively
As the pH become higher than the isoelectric point, it happens when acids is added in the system. The amino acids become _______ charge.
negatively
Four different functional groups are attached to it
Chiral carbon
four different functional group are attached to it
CHIRAL CARBON
because of this property, the alpha/chiral carbon is assymetric
STERIOCHEMISTRY
all of the functional groups are the same, but the location of the functional groups are mirror images but non-superimposable
ENANTIOMERS
amino acids can exist as enantiomers, they exhibit optical property known as
OPTICAL ACTIVITY
determined by the use of POLARIMETER
OPTICAL ACTIVITY
positive for dextrorotatory
clockwise
negative for levorotatory
counter clockwise
capacity to interact with water
polarity
hydrophobic
Non-Polar Amino Acids
water-fearing
non-polar amino acids
1 amino, 1 carboxylic, and a side chain that polar but neutral
polar neutral amino acids
1 amino acids, 2 carboxyl group
Polar Acidic Amino Acids
2 amino groups. 1 carboxyl group
Polar basic amino acid
Generally soluble in water
Amino acids
Insoluble in non-polar organic solvents
Amino acids
Crystal in solids with high melting point
Melting points
200-300 *c
Melting point
Tastes of amino acids
- sour or umami
- tasteless (leu)
- sweet (gly,ala,val)
- bitter (arg, lle)
Sweet or bitter taste
L-amino acids
Sweet flavor
D-amino acids
Formed by acid-base neutralization reaction
Salt formation
When a base reacts with an amino acid
Formation of salt with alkis
Chemical reaction that takes place in metabolic processes that involve enzymes
Decarboxylation
Removal of a carboxyl group from an amino acid
Decarboxylation
This takes place when an amino acids contains 2 carboxyl groups in the structure
Reaction with Ammonia
-nH2
Amino group
Formation of salt with an acid
Salt formation
The reactive amino group reacts with ninhydrin to form Ruhemanns’ purple
Reaction with nynhydrin
Quantitative determination of amino acids & proteins
Ninhydrin test
Transfer of an amino group from an amino acid to a keto acid to form a new amino acid catalyzed
Transamination
Transfer of an amino group from an amino acid to a keto acid to form a new amino acid catalyzed
Transaminases
Provides NH3+ for urea synthesis
Oxidative deamination