1. Explain why is malted barley used in this experiment rather than raw, unmalte

Question

1. Explain why is malted barley used in this experiment rather than raw, unmalted barley 2. What is the most important stabilizing force for secondary structures in proteins? 3. Ionic interactions are one type of noncovalent interaction in proteins. At physiological pH, this type of interaction can hold a carboxyl group and amino group of a protein together as shown below. ionic interaction (attraction between opposite charges) Use the chemical structures of a carboxyl and an amino group to show how these functional groups will be affected by a change to: a) Low pH b) High pH 147

Explanation / Answer

1.

Malted barley has the needed moisture content that is required to run the experiment as opposed to dry barley. Thus, malrted barley is used for thr given experiment.

2.

The most important bond for the secondary structure of protein is hydrogen bonding. Hydrogen bonding is strong bond which holds the protein chain in a particular geometry after folding.

3.

Ionic interaction between carbonyl group and amino group at physiological pH is shown above.

a.

at low pH, carboxyl groups are neutral and thus no more ionic interaction is seen.

b.

High pH : the carboxyl group is charged but the amine group is not uncharged and thus no ionic interaction is possible.

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