Mont globular proteins denature and lose their activity when briefly leated to 6.5 "C. However, globular proteins that contain multiple disulfide bonds ehen require longer heat exposure us higher temperatares to desumer them. One such protein is bov pancreatic trypsin inhibitor (BPTI). BPTI has 58 amino acid residues in a single peptile chain and contains three disulfide boeds. After cooling a solution of heat denabured BPT1, the protein requits its activity. What is the molecular buis for this property of BPTI? ◻ ◻ ◻ Dinalide bonds pervent the complete unbiling ef BPTI al ligh teneprahers. ◻ Divalitide bonds lower the optimal temperature of the martic BFTI partipuess is
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Most globular proteins are denatured and lose their activity when briefly heated to 65°C. However, globular proteins that contain multiple disulfide bonds often must be heated longer at higher temperatures to denature them. One such protein is bovine pancreatic trypsin inhibitor (BPTI), which has 58 amino acid residues in a single chain and contains three disulfide bonds. On cooling a solution of denatured BPTI, the activity of the protein is restored. What is the molecular basis for this property?
Madhur L.
(b) Most globular proteins are denatured and lose their activity when briefly heated to 65 8C. However, globular proteins that contain multiple disulfide bonds often must be heated longer at higher temperatures to denature them. One such protein is bovine pancreatic trypsin inhibitor (BPTI), which has 58 amino acid residues in a single chain and contains three disulfide bonds. On cooling a solution of denatured BPTI, the activity of the protein is restored. What is the molecular basis for this property?
Adi S.
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