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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. Characteristic of basic amino acids
have amino group in their side chains
pI
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
unsaturated fatty acid
2. Amino group placed on the right of a fischer projection is a?
will have pI of 6
D- amino acid
disulfide bond
modulates fluidity and seeks to maintain optimal fluidity
3. Polar amino acids
pyranose
serine - threonine - asparagine - glutamine - cysteine - tyrosine
glutamic acid and aspartic acid
pI
4. Enzyme that hydrolyzes maltose into 2 glucose molecules?
Beta pleated sheet
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
maltase
1. presence of strong acids 2. proteolytic enzymes
5. Diastereomers that vary in the configuration of 1 chiral center
glucose - alpha -1 -2- fructose
ketose
epimers
unsaturated fatty acid
6. Nonpolar - hydrophobic amino acids
anomeric carbon
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
peptide bonds and disulfide bonds
lactase
7. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
quaternary structure
Proteins
NH2CONH2
phospholipids
8. 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
Characteristics of the peptide bond
histidine - arginine - lysine
alpha helix
3 things about the cyclic form of a sugar as a hemiacetal
9. Energy storage molecule of carbohydrates for plants
amphipathic
unsaturated fatty acid
triacylglycerol
starch
10. Fxn of cholesterol in the membrane?
saturated fatty acid
have an R group that is polar enough to H bond - but does no acts an acid or a base
7.4
modulates fluidity and seeks to maintain optimal fluidity
11. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
anomers
Ka
histidine - arginine - lysine
1. presence of strong acids 2. proteolytic enzymes
12. 2 reasons why fats have more efficient energy stores than carbs
isomers
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
cysteine and methionine
packing and energy content
13. Name for 5 membered ring
furanose
glucose - alpha -1 -2- fructose
isoelectric point
have amino group in their side chains
14. Energy storage molecule of carbohydrates for animals
glycogen
packing and energy content
amphoteric
ketose
15. Glycosidic linkage of sucrose
glycogen
glucose - alpha -1 -2- fructose
7.4
serine - threonine - asparagine - glutamine - cysteine - tyrosine
16. The amino acid sequence of a protein that is determined by peptide bond
lipases
anomeric carbon
addition of water across of a bond
primary structure
17. Glycosidic linkage of cellulose
amphoteric
glucose - beta -1 -4- glucose
L- configuration
pyranose
18. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
have amino group in their side chains
triacylglycerol
ketose
2 things about the cyclic form of a sugar as an acetal
19. Fatty acid structure
peptide bond
starch
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
has thiol group that allows it the form disulfide bond
20. Name for 6 membered ring
glucose - alpha -1 -4- glucose
L- configuration
pyranose
3 things about the cyclic form of a sugar as a hemiacetal
21. Unique feature of cysteine
phospholipids
has thiol group that allows it the form disulfide bond
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
1. presence of strong acids 2. proteolytic enzymes
22. 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
peptide bonds and disulfide bonds
alpha helix
Characteristics of the peptide bond
glucose - beta -1 -4- glucose
23. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
Cause of Amino acid separation in gel electrophoresis
optical activity
peptide bonds and disulfide bonds
1. presence of strong acids 2. proteolytic enzymes
24. Unique feature of glycine
peptide bonds and disulfide bonds
only achiral amino acid
peptide bond
alpha helix
25. 4 causes of denaturation of proteins
van der Waal forces of hydrophobic tails
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
galactose - beta -1 -4- glucose
isoelectric point
26. Interconversion btw two anomers
galactose - beta -1 -4- glucose
aldose
serine - threonine - asparagine - glutamine - cysteine - tyrosine
mutarotation
27. 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
NH2CONH2
triacylglycerol
secondary structure
peptide bond
28. Unique feature of proline
only amino acid that his a secondary amine
L- configuration
modulates fluidity and seeks to maintain optimal fluidity
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
29. Molecule can act as a base and as an acid
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
Ka
amphoteric
2 things about the cyclic form of a sugar as an acetal
30. Epimers of sugars that vary in the configuration of their anomeric carbons
have amino group in their side chains
only achiral amino acid
anomers
Proteins
31. 3 carbon triol that forms backbone of triacylglycerol
histidine - arginine - lysine
glycerol
the basic precursor of the molecule (L or D glyceraldehyde)
primary structure
32. Fatty acid w/ no double bonds and maximum number of hydrogens
stereoisomers
saturated fatty acid
amphoteric
the basic precursor of the molecule (L or D glyceraldehyde)
33. (+) and (-) describe what?
optical activity
2 things about the cyclic form of a sugar as an acetal
histidine - arginine - lysine
amphoteric
34. Acidic amino acids
glutamic acid and aspartic acid
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
cysteine and methionine
have amino group in their side chains
35. Characteristics of hydrophobic amino acids
CH3COOH
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
absolute configuration
36. What kind of lipids compromise the lipid bilayer?
phospholipids
glutamic acid and aspartic acid
peptide bond
anomeric carbon
37. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
have acidic carboxylic acid on side chains - w/ pKa around 4
will have pI of 6
disulfide bond
3 things about the cyclic form of a sugar as a hemiacetal
38. What configuration do all naturally occuring amino acids have?
glutamic acid and aspartic acid
L- configuration
primary structure
parallel beta sheet
39. Hydrolysis
addition of water across of a bond
C3H6O3 - with one chiral center
pyranose
Ka
40. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
isomers
stereoisomers
amphipathic
1. presence of strong acids 2. proteolytic enzymes
41. 3 physiological roles of lipids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
Proteins
pI
secondary structure
42. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
anomeric carbon
L- amino acid
NH2CONH2
43. PH at which the amino acid has a net neutral charge
isoelectric point
the basic precursor of the molecule (L or D glyceraldehyde)
only amino acid that his a secondary amine
van der Waal forces of hydrophobic tails
44. Glyceraldehyde
cysteine and methionine
isoelectric point
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
C3H6O3 - with one chiral center
45. Hydrophilic amino acids
only amino acid that his a secondary amine
have amino group in their side chains
antiparallel beta sheet
all acidic - basic - and polar amino acids
46. Sugar with a carbonyl group at the 2 carbon position
ketose
D- amino acid
quaternary structure
L- configuration
47. Formula for urea
pyranose
L- amino acid
NH2CONH2
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
48. 2 covalent bonds formed in proteins
NH2CONH2
Ka
lipases
peptide bonds and disulfide bonds
49. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
tertiary structure
D- amino acid
glucose - alpha -1 -2- fructose
amphipathic
50. Sulfur containing amino acids
cysteine and methionine
unsaturated fatty acid
all acidic - basic - and polar amino acids
quaternary structure