Is there is any significance for the absence of disulfide linkages and heatsensitive typtophan residues in protein?

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Melese Temesgen

yes Cysteine is fomed due to reduction of two Cystine and the

disulfide linkages are very important properties of protein

tryptophan is not only heat sensitive also acid sensitive due to the charge not due to disulfide linkages .

Ashwini Kumar Dubey

Dear Dr. Rashmi,

Disulphide bonds play important roles in protein folding and its stability. The cysteine disulphide bonds are usually in extracellular secreted proteins.

The nonpolar and hydrophobic tryptophan residues contribute to the hydrophobic interaction during protein folding. Generally the hydrophobic moieties of an amino acid is present in the interior/core of a protein molecule.

With regards,