Biotechnology Forums

(04-01-2017, 01:26 AM)supriyo banerjee Wrote: [ -> ]May be the answer is : d.. bcz of salt bridge made of by the hydrogen bond and we knw H- bonding highly stable...for that reason last one is the answer...what is the answer???

I couldn't find the answer....
Could you please explain?

(04-01-2017, 01:26 AM)supriyo banerjee Wrote: [ -> ]May be the answer is : d.. bcz of salt bridge made of by the hydrogen bond and we knw H- bonding highly stable...for that reason last one is the answer...what is the answer???

I think the answer would be-
© increase in water of hydration.....
Because due to same CD value (a) is impossible......
As both are equally susceptible to hydrolysis in the presence or absence of reducing agent, the disulfide bonds are same for both.....So (b) is excluded....
As amino acid composition is 95% similar, there will be almost same number of amino acids with positively and negatively ​charged amino acids contributing same number of salt bridges...So option (d) is not possible....


Rest is option ©.....


Is my logic correct or not.....Please let me know......
Thank you....

But we cant say either the amino acid residue made up of by cystine or not...if it is thn your answer is no doubtly ture bcz we knw disulfide bond is covalent bond which is more stable...but disulfide bond in protein is very rare nd its unstable in cytosol for that reason methonine couldnt form the disulfide bridge and only stabilized by hydrogen bonding...if we see the ratio of the protein stability...most of the protein stable by the hydrogen bond or hydrophobic interaction...in salt bridge there are two types of effect are present one electrostatic interaction and one is hydrogen bonding which rise the stability of super impose molecular structure...so i think T consits a super impose molecular structure...for tht reason option D..

Plz let me knw im correct or wrong...

(04-01-2017, 07:05 PM)supriyo banerjee Wrote: [ -> ]But we cant say either the amino acid residue made up of by cystine or not...if it is thn your answer is no doubtly ture bcz we knw disulfide bond is covalent bond which is more stable...but disulfide bond in protein is very rare nd its unstable in cytosol for that reason methonine couldnt form the disulfide bridge and only stabilized by hydrogen bonding...if we see the ratio of the protein stability...most of the protein stable by the hydrogen bond or hydrophobic interaction...in salt bridge there are two types of effect are present one electrostatic interaction and one is hydrogen bonding which rise the stability of super impose molecular structure...so i think T consits a super impose molecular structure...for tht reason option D..

Your logic is also seeming to be correct..... and I am now confused.....
The two proteins are differed by only 5% amino acid composition... So will this 5% make a difference in saltbridge interaction?

From whr u got th question like tht

Send the link...i wnt to solve more..so tht i can improve my logic..

(04-01-2017, 07:28 PM)supriyo banerjee Wrote: [ -> ]Send the link...i wnt to solve more..so tht i can improve my logic..

This is a question from CSIR NET December 2014.....

Answer this question please.....
Two experiments were performed. In the first one, okazaki fragments were prepared from a replicating cell of E. Coli grown in the presence of 32P. In the other, the two strands of E. Coli chromosome were separated into a H strand and L strand, immobilized onto a nitrocellulose membrane and hybridized with the okazaki fragments prepared in the first experiment. Which one of the following options correctly describes the observation?

1. Okazaki fragments will hybridize to only Have strand

2. Okazaki fragments will hybridize to only L strand

3. Okazaki fragments will hybridize with both H and L strands

4. Because the H and L strands have been prepared from different cultures of E. Coli, the okazaki fragments will hybridize to neither