L4 Proteins Flashcards
Each amino acids has a _____ group, a ______ group, and a _______.
carboxyl
primary amino
side chain
Non polar aliphatic amino acids are _____. Hydrophobicity _____ as the number of carbon atoms on the hydrocarbon chain ______.
hydrophobic
increases
increases
Most aliphatic AA are found within protein molecules but _____ and _____ are found either inside or outside a protein molecule.
alanine
glycine
Examples of non polar aliphatic AA
-Alanine
-Glycine
-Proline
Branched chain
-Valine
-Leucine
-Isoleucine
Examples of aromatic amino acids
-Phenylalanine & tryptophan ( hydrophobic)
-Tyrosine ( X hydrophobic )
AA with side chains that contains _____ group or ____ group can be classified as aliphatic, polar, uncharged amino acids
amide ( asparagine , glutamine)
hydroxyl ( serine, threonine)
Examples of aliphatic, polar , uncharged AA are?
-Asparagine
-Glutamine
-Serine
-Threonine
Acidic AA composed of ____ acid and _____ acid. They are able to _____ protons ( hydrogen ) in reactions and becomes _____ charged. They are ______.
aspartic
glutamic
lose
negatively
hydrophilic
Basic AA has basic R chains that _____ to available _____ so they gain _____ charge.
bind
protons ( hydrogen )
positive
3 basic AA are?
arginine
lysine
histidine
Arginine has the ______ positive charge due to _______ nitrogen groups to synthesize proteins and catalyze enzyme function.
strongest
3
Histidine has a very _______ positive charge due to its lack of _____ in the amino group.
weak
nitrogen
Examples of sulfur containing AA ?
-Cysteine
-Methionine
Alpha ____ group of one AA reacts with alpha _____ group of another AA to form a _____ bond or CO-NH bridge
carboxyl
amino
peptide
2 AA form a _____
3 AA form a _____
4 AA form a _____
A few AA forms a ______
A combination of 10 to 50 AA forms a_____.
dipeptide
tripeptide
tetrapeptide
oligopeptide
polypeptide
Primary structure of protein is the ________________. The sequence of a protein is determined by the _______ that encodes the protein. Example is ______.
sequence of amino acids in a polypeptide chain
DNA of the gene
insulin
Secondary structure of protein refers to ______ structures that form within a ______ due to the interactions between ______ of the backbone. The most common types are _____ and _______. Both are held in shape by _____.
local folded
polypeptide
atoms
alpha helix
beta pleated
hydrogen bonds
Tertiary structure denotes _______ structure of the ______ protein. They are maintained by ________,______ and ______ forces.
three-dimensional
whole
hydrophobic bonds
electrostatic bonds
van der Waals
A covalent bond in tertiary structure called ______ keep parts of the polypeptide firmly attached to one another.
disulfide bonds
Quartenary structure of proteins is when polypeptides ______ to form ____ functional protein. Example is __________ and _______.
aggregates
one
hemoglobin
DNA polymerase
Hemoglobin carries _____ in the blood as made of _________ types.
blood
alpha and beta
What are the chemical and physical properties of protein?
-molecular weight
-solubility
-shape
-isoelectric pH
-precipitation reaction
-denaturation of proteins
Proteins can be classified into ______,____ and ______.
functions
solubility
nutritional value
Myoglobin is a ____ protein that stores ______ as a _____ against oxygen deprivation. It is a ____ protein composed of a ____ polypeptide chain that has one _______ binding site. Rich in ____ and ______.
monomeric
oxygen
reserve
globular
single
oxygen
alpha-helix
histidine
