Bio Chemistry Interview Questions
Questions Answers Views Company eMail

Why is it necessary to cleave proteins with at least two different reagents during sequencing?

1 1672

How are coupled reactions used in biochemistry?


Cells are in nonequilibrium, open systems. In what way is thermodynamics useful in this situation?

1 1754

What type of column is generally used to separate amino acids from each other?


Which properties of water are unusual for its size, and caused by hydrogen bonding?

1 1537

What kinds of proteins are involved in facilitating protein folding?

1 2014

What types of molecules can be purified via affinity chromatography?

1 1999

How can proteins be denatured and renatured?

1 2850

What does a sedimentation coefficient measure?

1 2010

How flexible are protein structures?

1 1657

What causes aromatic rings to stick to each other?

1 1717

How does H-bonding in the helix differ from that in the sheet?

1 1387

Why is the t-butyloxycarbonyl protecting group such a good choice for amino acid synthesis?


Why don’t all proteins have methionine as the N-terminal amino acid?

2 3586

How much empty space is found in globular proteins?

Bharat Biotech,


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Un-Answered Questions { Bio Chemistry }

what is meant by codan optimisation m rna enrichment?


Hi, I am venkat. I am done with M.Sc Medical Biochemistry in the year 2007. I got rejected 3 times at US consulate, and the reason they say is why are you going agian for PG when you have already done PG, and they are not ready to get convinced only on this issue.


Which compound is involved in reducing levels of homocysteine in the blood?


How are free energy changes related to enthalpy changes and entropy changes?


Where do hydrophobic and hydrophilic residues usually end up after protein folding?


why we use 96 well plate in ELISA plate reader?


A 3.00 * 10-6M solution in a 1.0 cm cuvette read 16 % T at 620nm. What were the absorbance and the molar absorbancy index of the solution?


How does hplc differ from normal column chromatography, and what are its advantages?


Describe the structure of a peptide giving the sequence.


When it functions as a "second messenger", cAMP a) acts outside the cell to influence cellular processes. b) acts "second in importance" to AMP. c) activates all cytosolic protein kinases. d) activates the cAMP-dependent protein kinase.


Why are right-handed helices more stable than left-handed helices?


what is QC and why is impotent in pathology lab


How are free energy changes related to LeChatelier's Principle?


why life span of RBC IS GREATER THEN THE WBC?


I understand that urine can act as a reagent to break disulfide bonds? I am particularly interested in bonds between cysteines. and or any other amino acids.