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Test your basic knowledge |
MCAT Organic Chemistry 2
Start Test
Study First
Subjects
:
mcat
,
science
Instructions:
Answer 50 questions in 15 minutes.
If you are not ready to take this test, you can
study here
.
Match each statement with the correct term.
Don't refresh. All questions and answers are randomly picked and ordered every time you load a test.
This is a study tool. The 3 wrong answers for each question are randomly chosen from answers to other questions. So, you might find at times the answers obvious, but you will see it re-enforces your understanding as you take the test each time.
1. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
glucose - beta -1 -4- glucose
optical activity
isomers
tertiary structure
2. Enzymes that hydrolyze fats
mutarotation
lipases
pI
will have pI of 6
3. Generated btw either thiols on different proteins or thiols on the same protein
2 things about the cyclic form of a sugar as an acetal
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
disulfide bond
D- amino acid
4. Enzyme that hydrolyzes maltose into 2 glucose molecules?
glucose - beta -1 -4- glucose
maltase
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
stereoisomers
5. Molecule can act as a base and as an acid
amphoteric
alpha helix
Ka
anomeric carbon
6. 4 causes of denaturation of proteins
galactose - beta -1 -4- glucose
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
aldose
7. Nonpolar - hydrophobic amino acids
anomers
phospholipids
NH2CONH2
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
8. 3 carbon triol that forms backbone of triacylglycerol
mutarotation
galactose - beta -1 -4- glucose
glycerol
lactase
9. Characteristic of basic amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
will have pI of 6
have amino group in their side chains
isomers
10. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
have amino group in their side chains
Beta pleated sheet
aldose
L- configuration
11. Glycosidic linkage of maltose
absolute configuration
glutamic acid and aspartic acid
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
glucose - alpha -1 -4- glucose
12. Formula for urea
mutarotation
NH2CONH2
van der Waal forces of hydrophobic tails
have an R group that is polar enough to H bond - but does no acts an acid or a base
13. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
pI
lipases
2 things about the cyclic form of a sugar as an acetal
serine - threonine - asparagine - glutamine - cysteine - tyrosine
14. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
glucose - beta -1 -4- glucose
anomeric carbon
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
antiparallel beta sheet
15. Acidic amino acids
glutamic acid and aspartic acid
have amino group in their side chains
Characteristics of the peptide bond
1. presence of strong acids 2. proteolytic enzymes
16. Amino group placed on the left of a fischer projection is a?
quaternary structure
CH3COOH
L- amino acid
addition of water across of a bond
17. Characteristics of acidic amino acids
disulfide bond
packing and energy content
have acidic carboxylic acid on side chains - w/ pKa around 4
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
18. Hydrophilic amino acids
pyranose
van der Waal forces of hydrophobic tails
primary structure
all acidic - basic - and polar amino acids
19. What stabilizes lipid bilayer?
glycogen
van der Waal forces of hydrophobic tails
L- amino acid
stereoisomers
20. What kind of lipids compromise the lipid bilayer?
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
disulfide bond
C3H6O3 - with one chiral center
phospholipids
21. Right handed helix w/ carboxyl of one amino acid bound to the amine of another amino acid three residues away - proline never resides in this structure b/c it would place a kink in the helix
alpha helix
aldose
L- amino acid
phospholipids
22. 2 reasons why fats have more efficient energy stores than carbs
D- amino acid
glucose - beta -1 -4- glucose
glucose - alpha -1 -4- glucose
packing and energy content
23. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
galactose - beta -1 -4- glucose
primary structure
L- amino acid
anomeric carbon
24. What configuration do all naturally occuring amino acids have?
pyranose
L- configuration
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
tertiary structure
25. 1. it exists in solution in equilibrium with linear form 2. mutarotation occurs readily 3. it is a reducing sugar - and reacts positively w/ Benedict's reagent
glucose - alpha -1 -4- glucose
epimers
3 things about the cyclic form of a sugar as a hemiacetal
van der Waal forces of hydrophobic tails
26. Characteristics of hydrophobic amino acids
mutarotation
amphipathic
anomers
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
27. Polar amino acids
2 things about the cyclic form of a sugar as an acetal
peptide bonds and disulfide bonds
triacylglycerol
serine - threonine - asparagine - glutamine - cysteine - tyrosine
28. Physiological pH
tertiary structure
7.4
Ka
Proteins
29. Covalent bond formed btw carboxyl group of one atom and the amino group of another amino acid in an addition - elimination mechanism - enzymes are required to carry out rxn
peptide bond
amphipathic
glucose - alpha -1 -4- glucose
C3H6O3 - with one chiral center
30. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
isoelectric point
Cause of Amino acid separation in gel electrophoresis
have acidic carboxylic acid on side chains - w/ pKa around 4
absolute configuration
31. Fxn of cholesterol in the membrane?
amphoteric
L- configuration
glycerol
modulates fluidity and seeks to maintain optimal fluidity
32. Amino group placed on the right of a fischer projection is a?
pI
1. presence of strong acids 2. proteolytic enzymes
D- amino acid
galactose - beta -1 -4- glucose
33. (R) and (S) describe what?
has thiol group that allows it the form disulfide bond
lipases
absolute configuration
mutarotation
34. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
tertiary structure
antiparallel beta sheet
Cause of Amino acid separation in gel electrophoresis
1. presence of strong acids 2. proteolytic enzymes
35. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
aldose
will have pI of 6
addition of water across of a bond
serine - threonine - asparagine - glutamine - cysteine - tyrosine
36. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
glycerol
secondary structure
cysteine and methionine
lactase
37. Unique feature of cysteine
lactase
has thiol group that allows it the form disulfide bond
pI
peptide bond
38. Interconversion btw two anomers
isomers
mutarotation
anomers
glutamic acid and aspartic acid
39. D and L describe what?
3 things about the cyclic form of a sugar as a hemiacetal
Characteristics of the peptide bond
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
the basic precursor of the molecule (L or D glyceraldehyde)
40. Acetic acid formula?
CH3COOH
starch
1. presence of strong acids 2. proteolytic enzymes
have amino group in their side chains
41. PH at which positive and negative charges balance to form a zwitterion
have an R group that is polar enough to H bond - but does no acts an acid or a base
maltase
pI
anomers
42. (+) and (-) describe what?
optical activity
7.4
D- glyceraldehyde
only amino acid that his a secondary amine
43. Energy storage molecule of carbohydrates for plants
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
unsaturated fatty acid
only achiral amino acid
starch
44. Fatty acid structure
glycerol
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
only achiral amino acid
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
45. Name for 5 membered ring
peptide bond
lactase
3 things about the cyclic form of a sugar as a hemiacetal
furanose
46. 3 physiological roles of lipids
amphoteric
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
have an R group that is polar enough to H bond - but does no acts an acid or a base
anomeric carbon
47. Basic amino acids
has thiol group that allows it the form disulfide bond
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
furanose
histidine - arginine - lysine
48. The amino acid sequence of a protein that is determined by peptide bond
lipases
epimers
D- amino acid
primary structure
49. Interaction btw polypeptide subunits arranged in polypeptide. can be covalent bonds or intermolecular forces - disulfide bond that does not form btw residues on the same protein affect (blank)
lipases
will have pI of 6
quaternary structure
triacylglycerol
50. Epimers of sugars that vary in the configuration of their anomeric carbons
pI
alpha helix
only amino acid that his a secondary amine
anomers