Give the name of the amino acid and state whether acidic, basic, neutral nonpolar/polar

D _____________________ ___________________
I _____________________ ___________________
Q _____________________ ___________________
K _____________________ ___________________
Y _____________________ ___________________
P _____________________ ___________________

Multiple Choice

+Which of the ff amino acids has two chiral carbons?

a.) P b.) I c.) Q d.) Y
+Which of the ff amino acids contains the isobutyl group in its side chain?
a.)L b.)I c.)V d.)N
+Which of the ff amino acids is S-containing?
a.)M b.)N c.)Q d.)S
+Which group consists only of amino acids with basic side chains
a.)leucine,lysine,histidine b.)arginine,leucine,histidine
c.)arginine,lysine,histidine d.)arginine, lysine,isoleucine
+Which amino acid is the precursor of the neurotransmitter serotonin?
a.)F b.)W c.)Y d.)S
+Which is not true in a peptide bond
a.) free rotation around peptide bond
b.) planar
c.) formed by elimination of water between amino acids
d.) basis of protein structure
+The order in which amino acids are linked in peptide/proteins is
a.) called the secondary structure of the peptide/protein
b.) from c-terminal to n-terminal
c.) from n-terminal to c-terminal
d.) in alphabetical order
+Which of the ff statements concerning protein structure is not true
a.) Primary protein structure of protein describes the unique sequence of amino acids in the
protein chain
b.) Secondary structre describes the peptide bonds joining the amino acids together in the
protein chain
c.) tertiary structure descrbies the overall 3 drimensional shape of protein
d.) Hydrogen bonding, disulfide bonds, salt bridges and van der Waals forces are responsible
for mainitng the tertiary structure or protein

+In a protein structure, the threonine side chain can participate in

a.) electrostatic interaction b.) hydrogen bond c.) disulfide bond d.) hydrophobic
interaction
+Which structural protein is found in bone, tendon, and skin
a.) collagen b.) fibrinogen c.) albumin d.) keratin
+Tuftsin is a peptide that stimulates and promotes the destruction of tumor cells. Its primary
structure is T-K-P-R. Which of the following is not a valid interpretation of its primary structure
a.) it is a tetrapeptide b.)Threonin is the n-terminal amino acid and Arginin is the C-terminala
amino acid c.) Carboxyl group of lysine is joined to the amino group of proline d.) amino
group of arginine is not joined to any other amino acid
+What is meant by the tertiary structure of the protein
a.) Refers to the peptide bond that join the amino acid together in protein chain
b.) Describes the regular, repeating structures found in protein chain
c.) describes the overall three dimensional shape of protein
d.) Describes the association of two or more polypeptide chains to form one functioning unit
+Hemoglobin and glycoprotein are two examples of proteins that contain a prostethic group.
What is a prostethic group
a.) a nonprotein group bonded to a protein to create a functional unit
b.) an inhibitor of the function of the protein
c.) a side chain of amino acid that is not one of the 20 standard amino acid
d.) an artificial amino acid that has been synthesized in the lab
+What term describes the type of b-pleated sheets in which both peptides are aligned from the
amino terminus to carboxy terminus
a.) antiparallel
b.) perpendicular
c.) parallel
d.) congruent
+A helix breaker
a.) G
b.)P
c.)F
d.)W
+Type of attractive force responsible for maintaining secondary structure of protein
a.) Hydrogen bonds between the carbonyl and amide groups of peptide bonds
b.) van der waals forces between the hydrophobic R groups of nonpolar amino acid
c.) salt bridges
d.)S-S bonds between thiol containing amino acids
+When a protein undergoes hydrolysis, which of the ff occurs
a.) peptide bonds are broken and individual amino acids are released
b.) protein folds into a functional, 3D shape
c.) water adds across each double bond that is present to give an alcohol
d.) new amino acids are joined to the growing protein chain
+Denaturation of a protein results in the loss of its native conformation and its biological activity.
The following best describes what happens when a protein is denature?
a.) the primary structure of the protein is altered
b.) peptide bonds are broken, and individual amino acids are released
c.) Secondary, tertiary, and quaternary levels of structures are disrupted
d.) The N-terminal and C-terminal ends of the protein are hydrolyzed
Chymotrypsin cleaves proteins selectiveley at
a.) K & N
b.) K & R
c.) W & Y
d.) F & T

Essay

Why is the peptide bond stronger and shorter that the normal C-N bond?

Explain the effect of protein conformation in:

1. Strong base
2. Detergents
3. High temperature

Aside from structural, storage, transport functions, give other functions of proteins and a specific
protein for each function

Difference of globular and fibrous based on its 3D shape

Explain briefly the disorder Ehlers-danlos syndrome

-Deduce the amino acid sequence:

1. Amino acid composition: A ​ ,D,F2,I,K,L,N,T,V
2. Caroboxy peptidase of decapeptide released D ​
3. Chymotrypsin yielded dipeptide of composition F ​ ,N​: tripeptide of ​D,I,L,​ and a
pentatpeptide with all the rest. Treatment of the tripeptide with PITC yielded ​PTH-I
4. Trypsin treatment of the decapeptide gave a tetrapeptide of composition F ​ ,N,K,T​; and a
hexapeptide with all the rest. Treatment of the hexapeptide with PITC gave ​PTH-V
Deduce amino acid sequence
1. Amino acid composition: ​A,E,G,N,R2,S,V2,Y
2. Carboxypeptidase treatement gave ​E
3. Trypsin treatment of the decapeptide gave a dipeptide of composition e ​ ,g ​a tripeptide of
composition ​A,N,R​; and a pentapeptide with all the rest. Treatment of the tripeptide with
2-4-DNFB gave ​DNP-N
4. Chymotrypsin treatment of the decapeptide yielded a dipeptide ​V,Y ​and an octapeptide
with all the rest. Treatment of the octapeptide with 2,4-DNFB gave D​ NFB-S