Myoglobin and haemoglobin structure: helices and haem group

1. 1there are 8 [blank_start]alpha helices[blank_end] making up 75% of the chain of myoglobin and [blank_start]5 non-helical[blank_end] structures between the helices.

   1. Aalpha helices
   2. B5 non-helical
2. 2the turns in myglobin and haemoglobin contain [blank_start]proline[blank_end], which has a unique [blank_start]ring[blank_end] structure

   1. Aproline
   2. Bring
3. 3conjugated proteins contain a [blank_start]prosthetic[blank_end] group and a polypeptide chain. In Myb and Hb this prosthetic group is a [blank_start]haem[blank_end] group

   1. Ahaem
   2. Bprosthetic
4. 4Haem contains four [blank_start]pyrrole[blank_end] rings linked to form a [blank_start]tetrapyrrole[blank_end] ring. the whole structure is known as a [blank_start]protoporphyrin[blank_end]

   1. Apyrrole
   2. Btetrapyrrole
   3. Cprotoporphyrin
5. 5in myoglobin the Fe2+ can form two additional bonds 1 above the plane of haem and one below

   1. AVerdadero
   2. BFalso
6. 6in haem the [blank_start]proximal histadine[blank_end] attached to [blank_start]F helix[blank_end] bonds with the Fe2+ whilst the [blank_start]distal histidine[blank_end] attached to the [blank_start]E helix[blank_end] stabilises 02 binding.

   1. Aproximal histadine
   2. BF helix
   3. Cdistal histidine
   4. DE helix
7. 7P50 at which myoglobin has lost half its 02 is [blank_start]3 mmHg[blank_end]

   1. A3 mmHg
8. 8haemoglobin is made of [blank_start]a1[blank_end], [blank_start]a2[blank_end], [blank_start]b1[blank_end] ,[blank_start]b2[blank_end] (in alphabetical order) subunits. they are all [blank_start]homozygous[blank_end] but the alpha and beta differ in only a few ammino acids

   1. Aa1
   2. Ba2
   3. Cb1
   4. Db2
   5. Ehomozygous

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certificate of higher education Biochemistry Test sobre Sin título, creado por David Fox el 14/05/2016.

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