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