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Archive for the ‘Proteins (Q)’ Category

Q: About Myoglobin

Posted by biochemistryquestions on September 27, 2008


 

(P-16) A characteristic of Myoglobin is that:

 

a)     the Hem is located in a hydrophilic environment

 

b)     it has primary, secondary, tertiary and quaternary structure.

 

c)      the iron in the Hem group is in Ferrous state

 

d)     it shows allosteric regulation

 

e)     it has four peptide chains.

 

 

Posted in Proteins (Q) | Tagged: , , | 1 Comment »

Q: About the structure of a membrane associated peptide

Posted by biochemistryquestions on September 24, 2008


 

(P-15) A 42-amino acids peptide related to the extracellular Alzheimer amyloid deposits has the last few residues immersed in the membrane bilayer. Based on your knowledge about membrane proteins, which of the following sequences most probably identifies the last five amino acids in this 42 residue peptide?

 

a)     Ala-Glu-Phe-Arg

 

b)     Val-Val-Ile-Ala

 

c)      Asp-Ser-Gly-Tyr

 

d)     Lys-Val-His-His-Gln

 

e)     Asp-Val-Gly-Ser

 

 

Posted in Proteins (Q) | Tagged: , , , , | Leave a Comment »

Q: About alpha-Helix structure

Posted by biochemistryquestions on September 21, 2008


Biochemistry Question P-14

 

Side view of an alpha-helix

Side view of an alpha-helix

 

 

 

 

 

This amino acid has a profound effect in the secondary structure of proteins, because when present in the amino acid sequence, it disrupts the a-helix structure:

 

a)     Alanine

 

b)     Glycine

 

c)      Proline

 

d)     Serine

 

e)     tryptophan

 

(The answer in this post)

 

Top view of an alpha-helix

Top view of an alpha-helix

 

Posted in Proteins (Q) | Tagged: , , | 4 Comments »

 
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