1- All the following amino acids have cyclic groups at their side chains except A-proline B-histidine C-aspartate

D-tryptophan 2- Which of the following can play a role in determining the conformation of a protein? A-ionic bonds B-hydrogen bonds C-hydrophobic interactions D-all of the above 3- Following the oxygenation of hemoglobin, the alpha & beta subunit move relative to one another, this describes a change in the............. Structure of the protein A-primary B-secondary C-tertiary D-quaternary 4- Which of the following statements about solutions of amino acids at physiological ph is true? A- All amino acids contain both positive & negative charges B - All amino acids contain positively charged side chains C- Some amino acids contain only positive charges D- All amino acids contain negatively charged side chains 5- Which of the following states of hemoglobin binds oxygen with the greatest affinity? A-HB(O)2 B- HB(O2)2 C-HB(O2)3 D-HB(O2)4 6-all the following forces may play a role in the formation of quaternary structure except A- Hydrogen bonds B-electrostatic interactions C-peptide bonds D-hydrophobic interactions 7- Concerning bonds that stabilize collagen, all of the following statements are correct except A-hydrogen bonds B- Satiric repulsion of proline-proline C-disulfide bond D-lysine-lysine covalent bond 8- Arg-Lys-Gly-Val: which of the following statements is NOT CORRECT regarding this structure A- it is a tetrapeptide B-trypsin treatment of it yields : Arg+Lys+Gly- Val C- it can be named : Arginyl-lysyl-glycyl-valyl D-it contains a net +2 charges

9- all of the following amino acids are found in proteins except A- threonine B- homocysteine C-Cysteine D- methionine 10 - a quaternary structure of human hemoglobin is best described as A- tetramer of identical subunits B-tetramer of 4 different subunits C- tetramer of 2 different subunits D- dimer of 2 myoglobin dimers 11-myoglobin has the following characteristics except : A- it is formed of a single polypeptide chain B- it has much higher affinity for oxygen than hemoglobin C- its protein part represents the quatemary structure D- it has no allosteric behavior 12- the binding of two R groups can give rise to a strong covalent bonds of the following combination A- systeine --- methionine B- tryptophan -- serine C- Cysteine -- Cysteine D- Valine --- leucine 13- which of the following amino acids contains three titratable groups A- glutamine B- glutamate C-asparagine D- tryptophan 14- the ground substance of the body is primarily composed of A-collagen B-keratin C-proteoglycans D-elastin 15- the oxygen affinity of adult hemoglobin is decreased by the following except A- 2,3 - bisphosphoglycerate B- carbon dioxide C- acetic acid D- atp 16- all of the following regarding myoglobin is correct except : A- it is formed of one polypeptide chain B- it has high affinity to oxygen C- it is present in muscles D- it has quaternary structure

17 - all of the following decrease the affinity of hemoglobin to oxygen except A- increase hydrogen ion concentration B- increase oxygen concentration C- increase CO2 concentration D- 2,3 - biphosphoglycerate 18- all of the following about alpha helix are true except A- proline disrupts the alpha helix structure B- there are 3.6 amino acid residues per turn C- alpha - hellix are mostly left handed D- hydrogen bonds are formed beteween peptide bonds every 4th amino acid 19- a galactose molecule is attached to collagen at residue of A- tyrosine B- serine C- threonine D- hydroxylysine 20- which of the folloing is non-protein amino acid A- arginine B- histidine C- ornithine D- glycine 21 - at netural ph , amixture of amino acids in solution would be predominantly A- nonpolar molecules B- dipolar ions C-postive & monovalent D- negatve & monovalent 22- which of the designations below best describes the relationship of subunits in the quaternary structure of adult hemoglobin A- ( alpha 1- alpha2 ) - ( beta 1 - beta 2 ) B- alpha - beta - beta - alpha C- Alpha 1- aplha 2 - beta 1 - beta 2 D- ( alpha 1 - beta 1 ) - ( alpha 2 - beta 2 ) 23- which of the following amino acids is the most compatible with an alpha-helical structure A- tryptophan B-lysine C-alanine D- proline

24- the concentration of hydrogen ion in solution is expressed as the PH , which is numerically equivalent to A. log [ H+] B. - log [ H+] C. Ln [ H+] D. L/log [ H+]

25- which of the following statemens about the peptide bond is true A- it is carbon ---- carbon bond B- it has cis hydrogen & oxygen groups C- it is found in fatty acids D- it is planar 26- emphysema can be due to inherited defect in A- collageenase B- elastase C- ascorbate D- alpha1-antitrypsin 27 - a bond that contributes to forming the secondary structure of protein but not the primary structure is A- ionic B- peptide C-hydrogen D-hydrophobic 28 - myoglobin A- has low affinity towwards O2 B- has high affinity towards O2 C- its affinity towwards o2 is affected by PO2 D- it has quaternary structure

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Define primary structure of proteins ?

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In the following polypeptide select the appropriate number for each type of amino acids

A. Aromatic amino acids ( ) B. Peptide bond ( ) C. Carboxy terminal end ( ) D - non polar branched - chain amino acid ( E- amino terminal end ( ) F- polar uncharged amino acid ( ) G- polar charged amino acids ( ) H. Sulfur - containing amino acid ( )

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List three forces stabilizing tertiary structure of protein

List three causes of protein denaturation

List three allosteric effectors affecting hemoglobin affinity to oxygen

From the above box fill the following table

Sulfur containing amino acids Aromatic amino acids Negatively charged amino acids Positively charged amino acids Polar uncharged amino acids Ketogenic amino acids Glucogenic and ketogenic amino acids

Compare between the following

Alpha helix structure Polypeptide shape Hydrogen bonds R- groups

Fill in the spaces with correct terms ( E helix - proximal - A helix - distal - F helix )

Beta sheet

When O2 binds to the heme , it pulls the ferrous into the plane of the porphyrin ring causing the ............ Histidine to move else This causes shift the position of the ........... Which becomes closer to the .................

The above oxygen dissociation curve of hemoglobin shows the effect of co2 1- which of the 2 curves ( right or left ) is due to high CO2 level ( ) 2- mention the effect of CO2 on the affinity of HB to oxygen ( ) 3-explain the mechanism of this effect

A- the arrow point to a molecule called ........ B- this molecule arises as a product from ....... This level of substance increase in case of ........... & ...........