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प्रश्न
Explain denaturation of proteins.
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उत्तर
- Denaturation is the process by which the molecular shape of protein changes without breaking the amide/peptide bonds that form the primary structure.
- High temperature, acid, base and even agitation can disrupt the noncovalent interactions responsible for a specific shape of the protein. This is referred to as the denaturation of proteins.
- Denaturation results in disturbing the secondary, tertiary, or quaternary structure of the protein. This causes a change in the properties of protein and the biological activity is often lost.
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संबंधित प्रश्न
Select the most correct choice.
A disulphide link gives rise to the following structure of a protein.
Give scientific reasons:
α-Amino acids have high melting points compared to the corresponding amines or carboxylic acids of comparable molecular mass.
Give scientific reasons:
On boiling egg albumin becomes opaque white.
Write the names and schematic representations of all the possible dipeptides formed from alanine, glycine and tyrosine.
Draw a neat diagram for the following:
Zwitter ion
Draw a neat diagram for the following:
Enzyme catalysis
The optically inactive α-amino acid among the following is _____________
Write the structure of Zwitterion of alanine.
Write the number of chiral carbon atoms present in fructose.
Complete the following reaction.
\[\ce{H2N - CH2 - COOH + H2N - CH2 - CH2 - COOH ->[-H2O] ?}\]
Define peptide bond.
Write types of proteins depending upon molecular shape.
Draw the structure of Haworth formula of sucrose.
Explain the primary structure of proteins.
____________ is NOT a simple protein.
Pyrimidines are ______.
Histones are involved in packaging of DNA into structural units called ______.
Read the following statements and select the correct option.
- In quaternary structure, the peptide chains are much looped, twisted, and folded back on themselves due to formation of hydrogen bonds.
- When a protein has more than two polypeptide subunits their arrangement in space is called secondary structure.
Identify the option that correctly describes the amphoteric nature of proteins.
Identify (i) and (ii) and select the correct option.
i. Protein portion of the enzyme is called the ____________.
ii. Non-protein constituent binding to the enzyme is called as the ____________.
The optically inactive amino acid is ____________.
Which of the following contains keratin?
Proteins are ______ of amino acids.
Identify the enzyme X in the following reaction.
\[\ce{H2O2(aq) ->[x] H2O(l) + \frac{1}{2} O2(g)}\]
The bacteriostatic antibiotic from the following is ______.
For the conversion of oxygen to ozone in the atmosphere, nitric oxide in gaseous phase acts as ______.
The side chain R in cysteine is ____________.
The enzyme which converts maltose to glucose is ______.
Which of the following amino acid is an essential amino acid?
Which of the following is the simplest amino acid?
The molecular weight of hemoglobin is ______ Daltons.
The number of proteins in an average human cell is over ______.
The most abundant cellular protein is ______.
A protein is a sequence of amino acids. The end of the polypeptide chain of -NH2 end and at -COOH end are respectively called ______.
An iron-containing red protein is ______
Which among the following is a globular protein?
Identify the side chain –R present in amino acid lysine.
The central dogma of molecular genetics states that the genetic information flows from:
Among the following the achiral amino acid is:
The secondary structure of a protein refers to ____________.
Which of the following statement is not correct?
Which of the following amino acids is achiral?
Give the differences between the primary and secondary structure of proteins.
Write the Zwitter ion structure of alanine.
Write the structure of all possible dipeptides which can be obtained from glycine and alanine.
The amino acid, which is basic in nature is ______.
Which among the following enzymes hydrolysis starch?
Tertiary structure of protein is stabilised by ______.
Peptide and hydrogen bonds are present in the primary structure of the protein which is due to ______.
The tightly bound non-proteinaceous organic compound in enzyme is ______.
Write a short note on peptide bond.
Write a short note on peptide bond.
Write a short note on peptide bond.
Write a short note on peptide bond.
Write a short note on a peptide bond.
Write the Zwitter ion structure of alanine.
Write the Zwitter ion structure of alanine.
Write a short note on peptide bond.
Write a short note on peptide bond.
Write a short note on peptide bond.
Write a short note on peptide bond.
Write the Zwitter ion structure of alanine.
Given below are two statements.
Statement I- Most of the blood proteins are acidic proteins.
Statement II - Derived proteins are not found in nature.
In the light of above statements, Select the correct option given below.
Which from following amino acids contains heterocyclic ring at a side chain (R) group?
In large proteins, peptide chains are much looped, twisted and folded back on themselves. The folded structure is due to the formation of ______ bonds.
The number of amino groups in the amino acids present in amides is ______.
