Identify what test is being described: Refers to the breaking of peptide bonds that connect amino acids to compose protein ? A. Hydrolysis B. Denaturation C. Heat denaturation D. Organic solvent denaturation E. Biuret test F. Hopkins – Cole Reaction G. Millon’s test H. Ninhydrin Test I. Sulfur test J. Xanthroproteic Test K. Chromatography L. Paper chromatography M. Competitive inhibition N. Noncompetitive inhibition O. Rancidity P. Hydrogenation
Proteins
We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains thousands and thousands of proteins, each with specific functions. Some help in the formation of cellular membrane or walls, some help the cell to move, others act as messages or signals and flow seamlessly from one cell to another, carrying information.
Protein Expression
The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.
1. Identify what test is being described: Refers to the breaking of peptide bonds that connect amino acids to compose protein ?
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
2. Identify what test is being described: Test that detects the free amino group in amino acids ?
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
3. Identify what test is being described: A foreign substance, which is structurally similar to the substrate, competes for the active site of an enzyme ?
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
4. Identify what test is being described: Decreases the solubility of most globular proteins in water to such extent that they precipitate out of solution ?
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
5. Identify what test is being described: Produces brown or black color result on the lead acetate paper using methionine, cysteine or cysteine ?
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
6. Identify what test is being described: The reaction of this test is based on the ability of
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
7. Identify what test is being described: Peptide chains are disorganized because there is a cleavage of the H bonds and other linkages
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
8. Identify what test is being described: Separate different amino acids based on their varying solubility in two different solvents ?
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
9. Identify what test is being described: Used for protein precipitation ?
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
10. Identify what test is being described: The foreign substance binds on the enzyme’s other slit other than active site. ?
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
11. Identify what test is being described: Recognize the presence of hydroxyphenyl group in proteins ?
A. Hydrolysis
B. Denaturation
C. Heat denaturation
D. Organic solvent denaturation
E. Biuret test
F. Hopkins – Cole Reaction
G. Millon’s test
H. Ninhydrin Test
I. Sulfur test
J. Xanthroproteic Test
K. Chromatography
L. Paper chromatography
M. Competitive inhibition
N. Noncompetitive inhibition
O. Rancidity
P. Hydrogenation
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