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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
Write the names and schematic representations of all the possible dipeptides formed from alanine, glycine and tyrosine.
Draw a neat diagram for the following:
Secondary structure of protein
Draw a neat diagram for the following:
Enzyme catalysis
The chemical nature of peptide bond in proteins is ____________
Complete the following reaction.
\[\ce{H2N - CH2 - COOH + H2N - CH2 - CH2 - COOH ->[-H2O] ?}\]
Write types of proteins depending upon molecular shape.
Write industrial application of enzyme catalysis.
Explain globular and fibrous proteins with example.
Draw the structure of Haworth formula of sucrose.
Explain the primary structure of proteins.
Nucleotide differs from a nucleoside as it has ______
Identify the option that correctly describes the amphoteric nature of proteins.
Identify 'P' and 'Q' in the following table.
| Proteins | Role |
| immunoglobulin | P |
| Q | Blood clotting |
Choose the WRONG statement from the following.
The optically inactive amino acid is ____________.
Which of the following contains keratin?
The conjugate acid of \[\ce{CO^2-_3}\] is ____________.
Which of the following is NOT a protein?
Proteins are polypeptides with linear chains of i ______ linked by ii ______ bonds.
The bacteriostatic antibiotic from the following is ______.
β-pleated sheets of polypeptide chains are present in ______.
Which of the following amino acids has \[\ce{Me - S - CH2 - CH2 -}\] group in the side chain?
The enzyme which converts maltose to glucose is ______.
The amino acid having −CH3 as side chain is ____________.
Which of the following is the simplest amino acid?
The basic amino acid is ____________.
The molecular weight of hemoglobin is ______ Daltons.
The number of proteins in an average human cell is over ______.
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 ______
If side-chain group-R for amino acid is -CH2OH, identify the amino acid from following?
Which of the following molecules from a zwitter ion?
Which among the following amino acids has the lowest molecular mass?
Identify the side chain –R present in amino acid lysine.
The central dogma of molecular genetics states that the genetic information flows from:
In a protein, various amino acids linked together by ____________.
In aqueous solution of amino acids mostly exists in, ____________.
Among the following L-serine is:
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 a note on denaturation of proteins.
Define enzymes.
Which of the following amino acid is basic in nature?
The amino acid, which is basic in nature is ______.
Which among the following enzymes hydrolysis starch?
Tertiary structure of protein is stabilised by ______.
The tightly bound non-proteinaceous organic compound in enzyme is ______.
Write a short note on peptide bond.
Write the Zwitter ion structure of alanine.
Define the term Protein.
Write the Zwitter ion structure of alanine.
Write a short note on a peptide bond.
Write a short note on peptide bond.
Short Answer Question.
Write the Zwitter ion structure of alanine.
Write a short note on peptide bond.
Write a short note on peptide bond.
Write the Zwitter ion structure of alanine.
Which from following is an essential amino acid?
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 ______.
