1. Nobel Prize in Physiology or Medicine in

 

1.      
In 1943, Frederick Sanger received his doctorate
for his research project which studied the metabolism of lysine in animal body.
Further in 1943, he joined Albert C. Chibnall and his research group at the
biochemistry department in Cambridge and started working on sequencing of amino
acids of insulin. This research was successful, and Sanger thus determined the
amino acid sequence of chains A and B of bovine insulin in 1951 and 1953
respectively. He was awarded The Nobel Prize in 1958 for his work on the
determination of structure of insulin molecule.

 

 

2.      
                                 AQSOWCDEUVFRGBTNHYMKIZLP

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Ala-Gln-Ser-Pyl-Trp-Cys-Asp-Glu-Sec-Val-Phe-Arg-Gly-Asx-Thr-Asn-His-Tyr-Met-Lys-Ile-Glx-Leu-Pro

 

3.      
Edmond H. Fisher and Edwin G. Krebs won the Nobel Prize in
Physiology or Medicine in 1992 for their discovery in reversible protein
phosphorylation and its importance as biological mechanism.

The research:-

Fisher and Krebs
started studying the regulation of glycogen phosphorylase.

Step 1 – Purified
phosphorylase to get pure enzyme.

Step 2 – Grinding
of rabbit muscle, extracting in water and squeezing it in cheesecloth.

Step 3 –
clarifying the turbid extract by passing it through a battery of filter papers.

 

Observations: –
extracted muscle contained inactive phosphorylase, which when passed through a
filter paper, became activated. This is due to the contamination of filter
paper with calcium ions. Also, they proved that the filtered crude muscle
contained ATP by labelling it with ?-ATP32, which proved that radioactivity had
been incorporated in the isolated protein and was just phosphorylated.

 

Conclusion: –
Activation of phosphorylase required presence of Ca+, Mg +, ATP and kinase
enzyme.

 

Mechanism:-

They thus found the molecular mechanisms which
leads to the interconversion of the two forms of phosphorylase and hence termed
the process as reverse phosphorylation. Their research proved so by elucidating
various processes the phosphatases and kinases undergo that lead to the
reversal. They showed the following:

·        
The enzyme phosphorylase converts glycogen to glucose which
serves as a fuel for muscle contraction. This enzyme is activated by addition
of phosphate group carried out by protein kinase.

·        
Phosphorylase can be inactivated by the removal of the
phosphate group which is carried out by the enzyme phosphatase, thus reversing
the phosphorylation process.

·        
The regulation of phosphorylation and reverse phosphorylation
is well maintained balance between the phosphatases and kinases.

4.      
 Leu-Sec-Lys-His-Gly-Phe_Xaa-Asp-Ser-Ala-Gln-Trp-Glu-Arg-Glx-Thr-Tyr-Ile-Pro-Orn-Met-Asn-Val-Cys

 

 

LUKHGFXDSAQWERZTYIPXMNVC

 

5.      
    

a.       SDEKAINVKWQLA
– neutral at physiological pH, charge = 0

b.       SDEKAINVKWQHA
– neutral at physiological pH, charge = 0

c.       SEERAINVAWQHA
–  negatively charged at physiological
pH, charge = -1

d.       SDEKAINVKWQEA
– negatively charged at physiological pH, charge = -1

e.       EEERAINVKWQKA
– neutral at physiological pH, charge = 0

 

Calculated the above charges based on
following:-

Amino Acid

Charge at physiological pH

Glutamic acid (E)

-1

Aspartic acid (D)

-1

Lysine (K)

+1

Arginine (R)

+1

Histidine (H)

0 (because pka is smaller than ph, hence it would be
deprotonated)

 

 

6.      
The following results were obtained when sequence alignment
of ?-hemoglobin and ?-hemoglobin was carried out using BLAST-

 

 

Identity in blast is the extent to which two
protein sequences are have the exact same residues at the same position in a
sequence alignment performed. Hence, it can be concluded from the above results
that these two sequences are similar. They have 43% similarity.

The bioinformatics tool, BLAST is very user
friendly and easy to use. Hence I did not run into any trouble while using it.

 

7.      
  Multiple ionizable functional
groups of Histidine at various pHs and charges.

 

 

8.        

Ala
(A)
Arg
(R) 
 Asn (N)  

Asp
(D)  
Cys
(C)  
Gln
(Q)  
Glu
(E) 
Gly
(G) 
His
(H) 
Ile
(I)
Leu
(L) 
Lys
(K) 
Met(M)

Phe
(F)  
Pro
(P)  
Ser
(S) 
Thr
(T)  
Trp
(W)  
Tyr
(Y)  
Val
(V) 
Pyl
(O)  
Sec
(U) 
 
(B)
(Z)
       (X)

14.8%
2.1%
       2.8%
5.6%
0.7%
0.7%
2.8%
4.9%
7.0%
0.0%
12.7%
7.7%
2.1%
4.9%
4.9%
7.7%
6.3%
0.7%
2.1%
9.2%
0.0%
0.0%
 
0.0%
0.0%
0.0%
 

 

Ala
(A)
Arg
(R) 
 Asn (N)  

Asp
(D)  
Cys
(C)  
Gln
(Q)  
Glu
(E) 
Gly
(G) 
His
(H) 
Ile
(I)
Leu
(L) 
Lys
(K) 
Met(M)

Phe
(F)  
Pro
(P)  
Ser
(S) 
Thr
(T)  
Trp
(W)  
Tyr
(Y)  
Val
(V) 
Pyl
(O)  
Sec
(U) 
 
(B)
(Z)
       (X)

 10.2%
  2.0%
  4.1%
4.8%
1.4%
2.0%
5.4%
8.8%
6.1%
0.0%
12.2%
7.5%
        1.4%
5.4%
4.8%
3.4%
4.8%
       1.4%
2.0%
     12.2%
0.0%
0.0%
 
0.0%
0.0%
0.0%
 

 

Amino acid composition of ?-hemoglobin                                       Amino
acid composition of ?-hemoglobin

Ala (A) Arg (R)   Asn (N)
Asp (D)
Cys (C)
Gln (Q)
Glu (E)
Gly (G)
His (H)
Ile (I)
Leu (L)
Lys (K)
Met(M)
Phe (F)
Pro (P)
Ser (S)
Thr (T)
Trp (W)
Tyr (Y)
Val (V)
Pyl (O)
Sec (U)
 
(B)
(Z)
(X)

8.26%
5.53%
4.05%
5.46%
1.37%
3.93%
6.73%
7.08%
2.27%
5.93%
9.65%
5.82%
2.41%
3.86%
4.72%
6.61%
5.35%
1.09%
2.92%
6.86%
0.0%
0.0%
 
0.0%
0.0%
0.0%
 
 

 

 

Average amino acid
composition of all UniProt/SwissProt Entries

 

 

It can thus be noted from above the tables that the amino
acid compositions of ?-hemoglobin and ?-hemoglobin are similar to each other.

Comparing it with the Uniprot/SwissBank entries, the
findings are-

 

·        
Neither the ? or ?
chain contain any Isoleucine.

·        
There is an abundance
of the non-polar aliphatic R group amino acids like glycine, lysine, leucine
etc. This can be explained by the hydrophobicity and non-polar nature,
increasing their folding in many forms.

 

 

Tools used:-

·        
BLAST

 

 

 

 

References:-

·        
https://www.ncbi.nlm.nih.gov/books/NBK62051/

·        

Reversible Protein Phosphorylation as a Regulatory Mechanism

·        
https://www.britannica.com/biography/Edmond-H-Fischer#ref267469

·        
https://www.ncbi.nlm.nih.gov/

·        
https://www.nobelprize.org/nobel_prizes/medicine/laureates/1992/press.html

·        
https://en.wikipedia.org/wiki/Frederick_Sanger