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