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Protein: Group 1 Abasolo, Banguiran, Boston, Carrillo, Haron, Lamban, Pajigal, Steenkamp Bsmls-2C

The document discusses protein structure and function. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It also discusses protein denaturation and how heat and heavy metals can disrupt the secondary and tertiary structures, though the primary structure remains intact. Several color reaction tests are described that can identify different amino acids or protein components, such as the Biuret test for peptide bonds.

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Keith Jason Cortes
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52 views14 pages

Protein: Group 1 Abasolo, Banguiran, Boston, Carrillo, Haron, Lamban, Pajigal, Steenkamp Bsmls-2C

The document discusses protein structure and function. It describes the four levels of protein structure: primary, secondary, tertiary, and quaternary. It also discusses protein denaturation and how heat and heavy metals can disrupt the secondary and tertiary structures, though the primary structure remains intact. Several color reaction tests are described that can identify different amino acids or protein components, such as the Biuret test for peptide bonds.

Uploaded by

Keith Jason Cortes
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Protein

GROUP 1
A B A S O L O , B A N G U I R A N , B O S TO N , C A R R I L L O , H A R O N , L A M B A N , PA J I G A L , S T E E N K A M P
BSMLS-2C
PROTEIN
• A naturally-occurring, unbranched polymer in which the monomer units are amino
acids.
•Proteins are most abundant molecules in the cells after water – account for about
15% of a cell’s overall mass.
•A protein is a peptide in which at least 40 amino acid residues are present
•Amino acid is an organic compound that contains both an amino group and
carboxyl group.
•The shape of a protein is very important to its function.
PROTEIN
•The shape of a protein is very important to its function.
1. PRIMARY STRUCTURE
◦ is the order in which amino acids are linked together in a protein. Primary protein structure always involves more than just the
numbers and kinds of amino acids present; it also involves the order of attachment of the amino acids to each other through
peptide bonds.

2. SECONDARY STRUCTURE
◦ is the arrangement in space adopted by the backbone portion of a protein. The two most common types of secondary structure are the
alpha helix (ɑ helix) and the beta pleated sheet (β pleated sheet).

3. TERTIARY STRUCTURE
◦ is the overall three-dimensional shape of a protein that results from the interactions between amino acid side chains (R groups) that are
widely separated from each other within a peptide chain

4. QUATERNARY STRUCTURE
◦ is the organization among the various peptide chains in a multimeric protein.
PROTEIN DENATURATION
Denaturation of proteins involves the disruption and possible destruction
of both the secondary and tertiary structures. Since denaturation reactions are
not strong enough to break the peptide bonds, the primary structure (sequence
of amino acids) remains the same after a denaturation process. Denaturation
disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a
random shape.
1) Effect of Heat
HEAT EXPECTED ACTUAL Procedure
• Place 2.0 mL egg white solution in a test tube (A)
• Place 2.0 mL of egg white solution in a test tube (B), heat in a
A - - boiling water bath for 5 minutes.
B ++ ++ • In tube 1 and 2, add 2.0 mL of egg white solution each. To test tube
1,add 95% ethanol. And to test tube 2, 70% ethanol.
ALCOHOL EXPECTED ACTUAL • Observe.
1 ++ ++
2 + +

++ = HEAVY PRECIPITATE
+ = SLIGHT PRECIPITATE
- =NEGATIVE
2) Effect of Heavy Metals
Procedures:
A. Add 2.0 mL of egg white solution to each of the 2 test  According to Hajeya Ali (2017). Denaturation of proteins
tubes and label 1 and 2 involves the disruption and possible destruction of both the
B. To test tube 1,Add 1.0 mL of 1% AgNO3 solution. to test secondary and tertiary structures.. The reaction of a heavy
tube 2 add 1.0mL of 10%. Mix well and note the color of metal salt with a protein usually leads to an insoluble metal
the precipitates formed. Set aside of 5 Minutes protein salt.
C. Decant the supernatant liquid and test the solubility of a
small portion of the precipitate in 5mL of Water
Expected Result:
Test tube 1 – white (not soluble)
Test tube 2 - Light Blue (slightly soluble)
COLOR REACTIONS
1. Xanthoproteic Test
2. Biuret Test
3. Ferric Chloride Test
4. Hopkins-Cole Test
5. Ninhydrin Test
6. Sakaguchi Test
7. Lead Acetate Test
Xanthoproteic Test
Reagents used:
 0.5ml Concentrated HNO3 Actual Result:
Nitric acid reacts with proteins to form yellow nitrated products. If
proteins that contain amino acids with aromatic rings are present, the
mixture turns yellow.
 12 drops 50% NaOH
Upon adding a base such as sodium hydroxide, the colour turns
orange. These colour changes are caused by nitrated aromatic rings in
the protein.
Expected Result:
The presence of concentrated nitric acid the solutions turns yellow upon
heating. The yellow colour turns orange by adding 50% NaOH to make
the solution alkaline.
Biuret Test
Biuret Test
23% Na2SO4
3 drops of blood plasma
6M NaoH - Sodium sulfate is used to precipitate the
- there to raise the pH of the solution to alkaline levels globulin in the blood.
0.5% CuSO4
Ether
-In the presence of peptide bonds, a copper (II) ions and nitrogen atoms
form mauve-colored co-ordination complexes when dissolved in alkaline - Is added to help separate the precipitate
solution.
-When peptide bonds are present in this alkaline solution, the Cu2+ions
during centrifugation.
will form a coordination complex with 4 nitrogen atoms from peptide
bonds. The complex of Cu2+ ions and nitrogen atoms make the color of Violet color indicates protein in the sample.
CuSO4 solution changes from blue to violet.
PURPLE/MAUVE COLOR indicates the presence of peptide bonds in the
sample.
Ferric Chloride Test
Reagents used: Actual Result:
5.0 mL of milk
5.0 gtts of FeCl3 solution
Expected Result: positive: Development of green color
negative: no color change (yellow)

Phenylpyruvic acid when reacts with ferric iron producing


a visible green color.
Hopkins-Cole Test
Reagents used:
2.0 mL of Hopkins-Cole reagent
1.0 mL of concentrated sulfuric acid
Expected Result:The purple ring at the junction indicates the presence of tryptophan
Actual Result:
Ninhydrin Test
-It can be used qualitatively (e.g. for chromatographic
visualization) or quantitatively (e.g. for peptide sequencing.
Reagents used:
Ninhydrin solution-is a chemical used to detect ammonia or
primary and secondary amines. When reacting with these
free amines, a deep blue or purple color known as
Ruhemann's purple
Purple from the start when taken out from the boiling water
bath, after 30 minutes it turns into cloudy
Sakaguchi Test
- A chemical test used for detecting the presence of Arginine.
Reagents used:
1.0mL of 10% NaOH Solution
1.0 mL of 2.0% a-naphthol solution
5 drops of sodium hypochlorite
What happens in this Test...
1. Egg white, NaOH and Naphthol solution is mixed.
2. NaOH needs to be added first because it’s colorless.
3. The Arginine reacts with a naphthol and an oxidizing agent such as bromine water or sodium hypochlorite to
give a red colored product
Lead Acetate Test
- The objective of this test is to detect the presence of amino acid containing sulfhydral
group.
Reagents used:
1.0mL 50% NaOH solution
Lead Acetate Solution
What happens in this Test...
1. The sulphur in the egg white is chemically bound in the organic molecules. The
NaOH dissolves the sulphur in the form of a soluble sodium sulphide solution
2. The reaction between the lead acetate solution and the Na2S produces a black
precipitate of lead sulphide and colourless sodium acetate in solution

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