SUBJECTS
|
BROWSE
|
CAREER CENTER
|
POPULAR
|
JOIN
|
LOGIN
Business Skills
|
Soft Skills
|
Basic Literacy
|
Certifications
About
|
Help
|
Privacy
|
Terms
Search
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. What describes the affinity of functional groups for a proton?
furanose
2 things about the cyclic form of a sugar as an acetal
peptide bonds and disulfide bonds
Ka
2. Enzymes that hydrolyze fats
lipases
mutarotation
L- configuration
epimers
3. Unique feature of proline
have acidic carboxylic acid on side chains - w/ pKa around 4
Ka
only amino acid that his a secondary amine
D- glyceraldehyde
4. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
galactose - beta -1 -4- glucose
have acidic carboxylic acid on side chains - w/ pKa around 4
stereoisomers
primary structure
5. Fatty acid w/ no double bonds and maximum number of hydrogens
saturated fatty acid
the basic precursor of the molecule (L or D glyceraldehyde)
C3H6O3 - with one chiral center
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
6. 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
3 things about the cyclic form of a sugar as a hemiacetal
addition of water across of a bond
aldose
all acidic - basic - and polar amino acids
7. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
primary structure
aldose
Proteins
will have pI of 6
8. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
peptide bond
L- amino acid
Characteristics of the peptide bond
secondary structure
9. Acetic acid formula?
CH3COOH
peptide bonds and disulfide bonds
aldose
NH2CONH2
10. Sugar with an aldehyde at the first carbon position
L- configuration
aldose
stereoisomers
galactose - beta -1 -4- glucose
11. Characteristics of polar amino acids
lipases
Ka
have an R group that is polar enough to H bond - but does no acts an acid or a base
Cause of Amino acid separation in gel electrophoresis
12. The amino acid sequence of a protein that is determined by peptide bond
tertiary structure
anomers
primary structure
peptide bond
13. 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
histidine - arginine - lysine
glucose - beta -1 -4- glucose
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
14. Epimers of sugars that vary in the configuration of their anomeric carbons
van der Waal forces of hydrophobic tails
anomers
D- amino acid
Proteins
15. D and L describe what?
the basic precursor of the molecule (L or D glyceraldehyde)
anomers
glucose - alpha -1 -4- glucose
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
16. Characteristics of acidic amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
anomers
serine - threonine - asparagine - glutamine - cysteine - tyrosine
amphoteric
17. Unique feature of glycine
only achiral amino acid
glucose - alpha -1 -2- fructose
stereoisomers
phospholipids
18. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
packing and energy content
tertiary structure
triacylglycerol
Cause of Amino acid separation in gel electrophoresis
19. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
lactase
amphipathic
has thiol group that allows it the form disulfide bond
Characteristics of the peptide bond
20. 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
furanose
glycogen
Characteristics of the peptide bond
21. 3 physiological roles of lipids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
tertiary structure
van der Waal forces of hydrophobic tails
glycerol
22. What configuration do all naturally occuring amino acids have?
maltase
pI
L- configuration
van der Waal forces of hydrophobic tails
23. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
amphipathic
pyranose
have an R group that is polar enough to H bond - but does no acts an acid or a base
tertiary structure
24. 2 reasons why fats have more efficient energy stores than carbs
packing and energy content
starch
maltase
will have pI of 6
25. Basic amino acids
histidine - arginine - lysine
C3H6O3 - with one chiral center
peptide bond
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
26. Fatty acid w/ one or more double bonds in cis form predominately
anomeric carbon
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
only achiral amino acid
unsaturated fatty acid
27. 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)
quaternary structure
glycogen
L- configuration
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
28. Glyceraldehyde
parallel beta sheet
C3H6O3 - with one chiral center
lipases
Proteins
29. Glycosidic linkage of maltose
cysteine and methionine
glutamic acid and aspartic acid
glucose - alpha -1 -4- glucose
galactose - beta -1 -4- glucose
30. Molecule can act as a base and as an acid
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
furanose
glucose - beta -1 -4- glucose
amphoteric
31. PH at which the amino acid has a net neutral charge
anomeric carbon
van der Waal forces of hydrophobic tails
D- amino acid
isoelectric point
32. Unique feature of cysteine
has thiol group that allows it the form disulfide bond
amphoteric
2 things about the cyclic form of a sugar as an acetal
antiparallel beta sheet
33. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
quaternary structure
2 things about the cyclic form of a sugar as an acetal
isomers
anomeric carbon
34. Fatty acid structure
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
epimers
histidine - arginine - lysine
35. Nonpolar - hydrophobic amino acids
saturated fatty acid
has thiol group that allows it the form disulfide bond
all acidic - basic - and polar amino acids
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
36. 3 carbon triol that forms backbone of triacylglycerol
phospholipids
pyranose
unsaturated fatty acid
glycerol
37. Amino group placed on the right of a fischer projection is a?
the basic precursor of the molecule (L or D glyceraldehyde)
D- amino acid
histidine - arginine - lysine
only achiral amino acid
38. Generated btw either thiols on different proteins or thiols on the same protein
epimers
maltase
disulfide bond
addition of water across of a bond
39. Polar amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
amphipathic
tertiary structure
glycerol
40. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
furanose
anomeric carbon
C3H6O3 - with one chiral center
saturated fatty acid
41. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
1. presence of strong acids 2. proteolytic enzymes
primary structure
CH3COOH
Characteristics of the peptide bond
42. Enzyme that hydrolyzes maltose into 2 glucose molecules?
maltase
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
anomeric carbon
furanose
43. Energy storage molecule of carbohydrates for plants
lactase
ketose
unsaturated fatty acid
starch
44. (+) and (-) describe what?
only achiral amino acid
triacylglycerol
optical activity
1. presence of strong acids 2. proteolytic enzymes
45. What stabilizes lipid bilayer?
peptide bonds and disulfide bonds
furanose
will have pI of 6
van der Waal forces of hydrophobic tails
46. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
Beta pleated sheet
glucose - beta -1 -4- glucose
optical activity
peptide bonds and disulfide bonds
47. What kind of lipids compromise the lipid bilayer?
phospholipids
CH3COOH
saturated fatty acid
ketose
48. Glycosidic linkage of sucrose
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
van der Waal forces of hydrophobic tails
glucose - alpha -1 -2- fructose
antiparallel beta sheet
49. 2 covalent bonds formed in proteins
peptide bonds and disulfide bonds
1. presence of strong acids 2. proteolytic enzymes
saturated fatty acid
will have pI of 6
50. (R) and (S) describe what?
van der Waal forces of hydrophobic tails
CH3COOH
mutarotation
absolute configuration