Chemistry, 20.09.2019 04:00 tylerjoshonti
You learned that a polypeptide in solution usually folds spontaneously into its proper three-dimensional shape. the driving force for this folding is the tendency to achieve the most favored thermodynamic conformation. a folded polypeptide can be induced to unfold (i. e., will undergo denaturation) if the solution is heated or made acidic or alkaline. the denatured polypeptide is a random structure, with many possible conformations.
(a) what is the sign of gibb's free energy change for the folding process?
(b) what is the sign of entrophy change for the folding process?
Answers: 2
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At a certain temperature the rate of this reaction is first order in hi with a rate constant of : 0.0632s2hig=h2g+i2g suppose a vessel contains hi at a concentration of 1.28m . calculate how long it takes for the concentration of hi to decrease to 17.0% of its initial value. you may assume no other reaction is important. round your answer to 2 significant digits.
Answers: 1
You learned that a polypeptide in solution usually folds spontaneously into its proper three-dimensi...
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