WorksheetsBC Lab: Exercise 5
Total questions: 36
Worksheet time: 20mins
Egg White is a clear liquid composed of
Water
Albumin
Globulins
Mucroproteins
What happen if you 3 Dimensional Proteins lose it shape?
It will be denatured
amino acids falls
it will separate the components having different chemical, physical composition
mixture of amino acids be seperated.
Denatured proteins is
Functional
Not Functional
Simpler Globular Proteins
Chiral
Proteins are held in their native conformations by a combination of forces of
hydrogen bonds
ionic interactions
disulfide bridges
hydrophobic interactions.
When it loses the 3D shape it will fall into a
Solution
Base
Soluble State
Insoluble State
Polymers of monomers amino acids
Protein
Amine Group
Albumin
Structure of Protein
it is soluble in water and dilute salts solutions such as isotonic saline.
Protein
Amino Acids
Proteins Structure
Amine Group
A typical protein may be composed of ______ of amino acids.
200
140
20
17
The R-groups of the amino acid may be
nonpolar
polar
positively charged
negatively charged
is any process that temporarily or permanently change the protein conformation which will result in a loss of protein activity.
Denaturation
Paper Chromatography
Biuret Test
Ninhydren Test
native conformation is usually the most water soluble, disrupt of what structures causes changes in solubility and frequently results in the formation of a solid in the solution.
Secondary Structure
Tertiary Structure
Primary Structure
Quaternary Structure
Is the linear sequence of amino acids present in a protein
Primary Structure
Secondary Structure
Tertiary Structure
Quaternary Structure
it refers to the shape, which along with peptides chain can exist
Secondary Structure
Primary Structure
Tertiary Structure
Quaternary Structure
the 2 most common secondary structure that stabilized by hydrogen bonding.
Aplha helix
Beta - Pleated Sheets
Beta Helix
Protein Receptors
Refers to the overall shape of simple protein molecules
Tertiary Structure
Primary Structure
Secondary Structure
Quaternary Structure
it is formed by several proteins structure
Quaternary Structure
Primary Structure
Secondary Structure
Tertiary Structure
Denaturing Agents includes:
Heat
Extreme of pH
Some Reagents
Salts of Metal ions
This causes atoms to vibrate more rapidly by kinetic energy that will disrupt relatively weak forces such as hydrogen bonds and hydrophobic interactions.
Heat
Extreme of pH
Some Reagents
Salts in metal ions
is used in sterilization to denature and hence destroy the enzymes in bacteria.
Heat
some reagents
Extreme of pH
Salts of metal ions
The R-groups in the amino acid chain are often charged and can form ionic bonds with a group of opposite charge
Extreme of pH
Heat
Some Reagents
Salts of Metal Ions
Chemicals like ethyl alcohol can form hydrogen bonds with protein molecules which will disrupt the hydrogen bonding within the molecule.
Some Reagents
Extreme of pH
Heat
Salts of metal ions
Does the Extremes of pH can change the charges on these positive and negative groups to disrupting ionic bonds.
True
False
Converse True
Converse False
A 70% solution of alcohol can be used as a disinfectant, because......
alcohol functions to denature the proteins in bacteria.
alcohol functions to denature the Carbon, Hydrogen in bacteria.
yeast eats fruit sugar to form ethanol
ethanol that turn to acids to evaporate
Disrupted disulfide bridges and salt linkages cause the protein to precipitate out of solution as an insoluble metal-protein salt, this make some of the heavy metal salts suitable for use as topical antiseptics.
Salt of metal ions
Heat
Extreme pH
Some Reagents
Substances high in protein, such as egg whites and milk, are used as
Antidote of Heavy metal poisoning
Antidote of Light Metal poisoning
Antidote for Arsenic poisoning
Universal Antidote.
egg whites and milk, are used as antidotes for heavy metal poisoning because,
because their proteins readily combine with the metal ions to form insoluble solids and this insoluble matter are immediately removed from the stomach by the use of an emetic to prevent the gastric juices from destroying the protein and once again liberating the poisonous heavy metal ions.
because their amine group readily combine with the non metal ions to form soluble solids and this soluble matter are immediately removed from the stomach by the use of an emetic to prevent the gastric juices from destroying the protein and once again liberating the poisonous heavy metal ions.
Stabalize the blood
Regulate the body temperature.
PROTEINS:
Presence of alkali
BIURET TEST
XANTHOPROTEIC TEST
NINHYDRIN TEST
MILLON'S TEST
PROTEINS:
BIURET TEST RESULTS
VIOLET
BLUE
YELLOW
BRICK RED
PROTEINS:
Presence of concentrated nitric acid
MILLON'S TEST
XANTHOPROTEIC TEST
NINHYDRIN TEST
BIURET TEST
PROTEINS:
Proteins react with ninhydrin solutions
NINHYDRIN TEST
BIURET TEST
MILLONS TEST
XANTHOPROTEIC TEST
PROTEINS:
NINHYDREN TEST
YELLOW
NO CHANGES
BLUE COLOR
ORANGE
PROTEINS:
XANTHOPROTEIC TEST
YELLOW
VIOLET
BLUE COMPLEX
NO PRECIPITATE
PROTEIN:
BRICK RED ON BOILING,
XANTHOPROTEIC TEST
MILLONS TEST OF ALBUMIN
MILLON TEST OF GELATIN
NINHYDREN TEST
PROTEINS:
NO PRECIPITATE OF SOLUBLE PROTEINS
MILLON TEST ALBUMIN
MILLON TEST GELATIN
XANTHOPROTEIC TEST
BIURET TEST
PROTEINS:
TO DETECT THE PRESENCE OF SOLUBLE PROTEINS.
MILLONS TEST
BIURET TEST
NINHYDREN TEST
XANTHOPROTEIC TEST
PROTEINS:
THE PRECIPITATE INDICATES THE PRESENCE OF TYROSINE RESIDUE.
MILLONS TEST ALBUMIN
MILLON TEST GELATIN
NINHYDREN TEST
BIURET TEST
