1. Hemoglobin and myoglobin both :
1)bind nem in a hydrophobic pocket
2)are highly alphahelical
3)bind one molecule of nem per globin chain
4)bind one 2,3bisphosphoglycerate per molecule
possible answers : a]2,3 b]1,2,3,4 c]3 d]1,4 e]1,2,3
1. If nem stands for oxygen, then false. The oxygen binding pocket contains a charged iron atom which binds to the lone pairs of the oxygen.
2. True, just look up the structures of the two molecules in a biochemistry text.
3. If nem stands for oxygen, then true. Although hemoglobin binds 4 oxygen molecules, it consists of four globin chains which each bind one oxygen.
4. False, myoglobin cannot bind BPG. BPG binds to the "hole" formed in the middle of the tetramer of hemoglobin chains. More on BPG here:
http://en.wikipedia.org/wiki/2%2C3-bisphosphoglycerate2.what is rate of enzyme reaction when the substrate concentraitor is ten times higher than its Km and maximum rate is 10v ?
1)9
2)8
3)10
4)0.9
5)0.1
Look up the Michaelis-Menten equation and just plug in your values.
3.active site of all serine proteases contain
1)Asp
2)Glu
3)His
4)Ser
This is a weird question, because the serine proteases contain a catalytic triad consisting of an aspatate, a histadine, and a serine. The negatively charged aspartate interacts with the histadine, increasing the pKa of the histadine (i.e. the his becomes more basic). This allows the histadine to deprotonate the serine, which creates an oxyanion capable of performing nucleophilic attack on the amide bond of a protien. So, options 1, 3, and 4 are correct.
More on serine proteases here:
http://en.wikipedia.org/wiki/Serine_proteaseSee catalytic mechanism especially.
BTW, these sets of questions should be in the biochemistry section.