Biochemistry Book for pharmacy Technician 1st year..
Biochemistry Aipg
Vitamins, Biochemistry, Nutrition
This book, as the title suggests, is an Outline of Biochemistry-principally mammalian biochemistry and not the full panoply of the subject. In other words. it is not an encyclopedia but, we hope, a...
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CLINICAL BIOCHEMISTRY Metabolic and clinical aspect THIRD EDITION By William J. Marshall Marta Lapsley Andrew P. Day Ruth M. Ayling Increasing integration between the pathology disc...
first year Biochemistry
Biology
this is a comprehensive collection of mcq in medical biochemistry, which is particularly useful for pg preparation and undergraduate revision.
MCQs of biochemistry
MCQ on Chromatography
biochemistry MCQ to practice
Full description
Experimental-biochemistry-pdf
1.
At the center of all 20 standard amino acids is what is termed the α -carbon
that is covalently
bonded with four other chemical groups. Which of these four chemical groups is not a normal component of all amino acids? A. an amino group B. a carboxyl group C. a side chain (R group) D. a methyl group 2. The isoelectric point, or pI, of an amino acid or a protein is A. the pH at which the amino acid or protein has no net charge. B. zero at pH 7.0. C. the pH at which the amino acid or protein is neither hydrophobic nor hydrophilic. D. the measure of how hydrophobic an amino acid or prot ein is. 3.
Peptide bonds, which covalently link two amino acids, result from A. the oxidation of amino acids. B. the condensation of amino acids. C. the hydrolysis of amino acids. D. hydrogen bonds between amino acids
4.
Which group or groups on a protein contr ibute most to its overall acid-base properties? A. The α -amino groups of all nonterminal amino
acids. B. The N-terminal α-amino group on the protein. C. The R groups on the protein. pr otein. D. The C-terminal α -carboxyl group on the protein. 5.
Which of the following is true about the Edman degradation system of se quencing polypeptides? A. The Edman degradation system will work on any size polypeptide. B. In the Edman degradation system the amino-terminal residue is labeled and the polypeptide is hydrolyzed to its constituent amino acids. C. In the Edman degradation system the amino-terminal residue is labeled, c leaved and identified in each successive cycle. D. The Edman degradation system is carried out on a mac hine called an edmanator.
6.
Enzymes are biological catalysts that enhance the rate of a reaction by: A. increasing the amount amount of free energy released B. decreasing the amount of free energy released C. increasing the energy of the transition state D. decreasing the activation energy
7.
The three-dimensional structure of macromolecules is maintained primarily through noncovalent interactions. Which of the following are not considered non-covalent interactions? interactions? A. hydrogen bonds B. van der Waals interactions C. amide bonds D. ionic interactions
8.
All of the amino acids that are found in proteins (except proline) contain a(n): A. carbonyl group B. carboxyl group
C. ester group D. 9.
amino group
Of the 20 standard amino acids, only ______ is not optically active. The reason is that its side chain _________. A. alanine; is a simple methyl group B. glycine; is unbranched C. lysine; contains only nitrogen. D. glycine; is a hydrogen atom
10. The side chains of nonpolar amino acids are best categorized as: A. hydrophobic B. positively charged C. negatively charged D. hydrophilic 11. Trypsin cuts primarily after what type of residue? A. aliphatic non polar B. negatively charged C. small uncharged D. positively charged 12. Which of the following may prevent Edman sequencing? A. C-terminal amidation B. phosphorylation C. blocked N terminal D. N-linked glycosylation Problem Solving
1. Identify the unknown hexapeptide from the following data: o complete hydrolysis gives equimolar amounts of Arg, Glu, Lys, Phe, Pro, Tyr o Edman degradation of the hexapeptide gives labeled Phe o chymotrypsin cleavage gives a tetrapeptide, Phe, and Glu o Edman degradation of the tetrapeptide gives labeled Lys o trypsin cleavage gives three dipeptides o Edman degradation of the dipeptides gives labeled Phe, Pro, and Tyr
