Why is it necessary to cleave proteins with at least two different reagents during sequencing?1 1491
Cells are in nonequilibrium, open systems. In what way is thermodynamics useful in this situation?1 1632
Which properties of water are unusual for its size, and caused by hydrogen bonding?1 1420
What kinds of proteins are involved in facilitating protein folding?1 1879
What types of molecules can be purified via affinity chromatography?1 1848
How can proteins be denatured and renatured?1 2638
What does a sedimentation coefficient measure?1 1871
How flexible are protein structures?1 1544
What causes aromatic rings to stick to each other?1 1620
How does H-bonding in the helix differ from that in the sheet?1 1286
Why don’t all proteins have methionine as the N-terminal amino acid?2 3438
How much empty space is found in globular proteins?858
All technical,written test questions
what is meant by codan optimisation m rna enrichment?
Calculate the molar extinction coefficient of a solution containing 5 *10-4 g litre-1 of a biomolecule, molecular weight 275 g mol-1, and absorbance 0.75 in a 1.2 cm cuvette.
How are coupled reactions used in biochemistry?
Compare and contrast feedback inhibition and enzyme repression?
Which vitamins participate, in coenzyme form, in reactions of the tricarboxylic acid cycle?
can i used antimony potassium tartrate against potassium tartrate in Fehling B solution ?
What is zone electrophoresis?
What are hydrophobicity scales, and how are they used?
how I cell disease is caused?
what is familiar hypercholesterolemia?
How are free energy changes related to enthalpy changes and entropy changes?
why ph is not more than 14?
Which compound is involved in reducing levels of homocysteine in the blood?
What factors are involved in determining the electrophoretic mobility of a molecule?