Multiple choice questions

[_Luna_]

Hey, I have some multiple choice questions that botherS me. I'll try translating them hoping someone could give me an answear.

1. Hydrophobic interaction in protein is giving important stabilization contributions

a) to proteins secundary- and tertiarystructure.
b) just to the orientation of polar amino acids
c) to the proteins primarystructure
d) after every possible hydrogenbonding are formed
e) only in hydrophobic fases

I am here guessing a or d, but I am very uncertain.

2. The structural membraneproteins are characterized in case of that they

a) don't transport small molecules
b) exist only by beta sheets
c) show prostetic carbohydrate groups on the cytoplasmatic side
d) have a hydrophobic transmembrane domain
e) constitue about 10% of the membrane proteins

Small molecules doesn't use transportproteins so it could be d, but again I'm not certain.

3. In watery solutions proteins conformation is decided by two factors: A maximum of the number of hydrogenbonding and:

a) a minimize av entropy by the formation of a watery shell around the protein
b) a rotation off polar amino acid residues out against the outer shell off the protein
c) a rotation off hydrophobic amino acids sidechains towards the centre of the protein
d) minimize off hydrophobic interactions
e) maximize of ion interaction

Here I actually don't have a clue, but someone told me it could be a?

[aftabac]

Hi
according to my view its
1-d
2-d
3-a

regards
aftab

[_Luna_]

Does somebody else have an answear to question 2?
Because I have read somewhere that structuralproteins can be divided into two groups where one is consisting of proteins with hydrophobic transmembrane domain.

In the formation from S to P will an enzyme change the equilbrium to the product?

And if a enzymreaction have a favourable equilibrium would it have a high reactionrate?

[aftabac]

Hi
well, enzyme dont change the equilibrium of the reaction but it speed up of a reaction so that equlibrium could be achieved early but it dont change the equilibrium of the reaction.
and 2ndly if the equlibrium is achieved easily or its favourable then definatly the reaction rate for that particular reaction is high.

regards
aftab

[appy]

Originally Posted by _Luna_

Hey, I have some multiple choice questions that botherS me. I'll try translating them hoping someone could give me an answear.

1. Hydrophobic interaction in protein is giving important stabilization contributions

a) to proteins secundary- and tertiarystructure.
b) just to the orientation of polar amino acids
c) to the proteins primarystructure
d) after every possible hydrogenbonding are formed
e) only in hydrophobic fases

I am here guessing a or d, but I am very uncertain.
its A

2. The structural membraneproteins are characterized in case of that they

a) don't transport small molecules
b) exist only by beta sheets
c) show prostetic carbohydrate groups on the cytoplasmatic side
d) have a hydrophobic transmembrane domain
e) constitue about 10% of the membrane proteins

Small molecules doesn't use transportproteins so it could be d, but again I'm not certain.
its d

3. In watery solutions proteins conformation is decided by two factors: A maximum of the number of hydrogenbonding and:

a) a minimize av entropy by the formation of a watery shell around the protein
b) a rotation off polar amino acid residues out against the outer shell off the protein
c) a rotation off hydrophobic amino acids sidechains towards the centre of the protein
d) minimize off hydrophobic interactions
e) maximize of ion interaction

Here I actually don't have a clue, but someone told me it could be a?

[sweetsunil21]

ya final answer is a

[wr_1a]

thanks