SUBJECTS
|
BROWSE
|
CAREER CENTER
|
POPULAR
|
JOIN
|
LOGIN
Business Skills
|
Soft Skills
|
Basic Literacy
|
Certifications
About
|
Help
|
Privacy
|
Terms
|
Email
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. Generated btw either thiols on different proteins or thiols on the same protein
peptide bond
disulfide bond
have amino group in their side chains
optical activity
2. Molecule can act as a base and as an acid
glucose - alpha -1 -2- fructose
amphoteric
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
L- configuration
3. 3 carbon triol that forms backbone of triacylglycerol
all acidic - basic - and polar amino acids
anomers
packing and energy content
glycerol
4. 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
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
secondary structure
cysteine and methionine
5. Name for 5 membered ring
furanose
isomers
7.4
histidine - arginine - lysine
6. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
modulates fluidity and seeks to maintain optimal fluidity
Characteristics of the peptide bond
glutamic acid and aspartic acid
3 things about the cyclic form of a sugar as a hemiacetal
7. Characteristics of polar amino acids
disulfide bond
have an R group that is polar enough to H bond - but does no acts an acid or a base
parallel beta sheet
optical activity
8. Fatty acid structure
L- amino acid
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
galactose - beta -1 -4- glucose
1. presence of strong acids 2. proteolytic enzymes
9. Diastereomers that vary in the configuration of 1 chiral center
absolute configuration
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
epimers
van der Waal forces of hydrophobic tails
10. Sugar with a carbonyl group at the 2 carbon position
ketose
aldose
saturated fatty acid
have an R group that is polar enough to H bond - but does no acts an acid or a base
11. Unique feature of cysteine
has thiol group that allows it the form disulfide bond
CH3COOH
furanose
galactose - beta -1 -4- glucose
12. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
addition of water across of a bond
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
tertiary structure
secondary structure
13. Fatty acid w/ no double bonds and maximum number of hydrogens
glucose - alpha -1 -4- glucose
7.4
saturated fatty acid
only achiral amino acid
14. What stabilizes lipid bilayer?
van der Waal forces of hydrophobic tails
peptide bond
1. presence of strong acids 2. proteolytic enzymes
Ka
15. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
peptide bond
ketose
triacylglycerol
modulates fluidity and seeks to maintain optimal fluidity
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
peptide bond
Characteristics of the peptide bond
van der Waal forces of hydrophobic tails
anomers
17. Epimers of sugars that vary in the configuration of their anomeric carbons
anomers
will have pI of 6
furanose
galactose - beta -1 -4- glucose
18. D and L describe what?
C3H6O3 - with one chiral center
cysteine and methionine
the basic precursor of the molecule (L or D glyceraldehyde)
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
19. Amino group placed on the left of a fischer projection is a?
D- amino acid
have amino group in their side chains
L- amino acid
furanose
20. What describes the affinity of functional groups for a proton?
cysteine and methionine
epimers
packing and energy content
Ka
21. Acetic acid formula?
L- amino acid
peptide bonds and disulfide bonds
only achiral amino acid
CH3COOH
22. Physiological pH
CH3COOH
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
7.4
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
23. Sulfur containing amino acids
cysteine and methionine
histidine - arginine - lysine
glycogen
2 things about the cyclic form of a sugar as an acetal
24. Characteristics of acidic amino acids
glycerol
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
have acidic carboxylic acid on side chains - w/ pKa around 4
have an R group that is polar enough to H bond - but does no acts an acid or a base
25. Interconversion btw two anomers
aldose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
addition of water across of a bond
mutarotation
26. Energy storage molecule of carbohydrates for animals
glycogen
furanose
saturated fatty acid
isomers
27. 2 reasons why fats have more efficient energy stores than carbs
packing and energy content
van der Waal forces of hydrophobic tails
alpha helix
maltase
28. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
disulfide bond
1. presence of strong acids 2. proteolytic enzymes
addition of water across of a bond
Characteristics of the peptide bond
29. Characteristic of basic amino acids
stereoisomers
1. presence of strong acids 2. proteolytic enzymes
anomers
have amino group in their side chains
30. (R) and (S) describe what?
7.4
absolute configuration
have amino group in their side chains
isoelectric point
31. Fatty acid w/ one or more double bonds in cis form predominately
amphoteric
optical activity
peptide bond
unsaturated fatty acid
32. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
isomers
serine - threonine - asparagine - glutamine - cysteine - tyrosine
antiparallel beta sheet
33. What kind of lipids compromise the lipid bilayer?
the basic precursor of the molecule (L or D glyceraldehyde)
phospholipids
furanose
glutamic acid and aspartic acid
34. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
packing and energy content
histidine - arginine - lysine
Proteins
glycogen
35. Basic amino acids
van der Waal forces of hydrophobic tails
CH3COOH
histidine - arginine - lysine
NH2CONH2
36. Sugar with an aldehyde at the first carbon position
aldose
secondary structure
saturated fatty acid
glucose - alpha -1 -2- fructose
37. Formula for urea
secondary structure
mutarotation
NH2CONH2
C3H6O3 - with one chiral center
38. Nonpolar - hydrophobic amino acids
Proteins
cysteine and methionine
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
maltase
39. 3 physiological roles of lipids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
have acidic carboxylic acid on side chains - w/ pKa around 4
serine - threonine - asparagine - glutamine - cysteine - tyrosine
40. 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
L- configuration
maltase
stereoisomers
41. Glycosidic linkage of maltose
mutarotation
maltase
Cause of Amino acid separation in gel electrophoresis
glucose - alpha -1 -4- glucose
42. PH at which the amino acid has a net neutral charge
isoelectric point
the basic precursor of the molecule (L or D glyceraldehyde)
only achiral amino acid
2 things about the cyclic form of a sugar as an acetal
43. Glycosidic linkage of lactose
amphipathic
2 things about the cyclic form of a sugar as an acetal
cysteine and methionine
galactose - beta -1 -4- glucose
44. Fxn of cholesterol in the membrane?
peptide bonds and disulfide bonds
histidine - arginine - lysine
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
modulates fluidity and seeks to maintain optimal fluidity
45. What configuration do all naturally occuring amino acids have?
L- configuration
phospholipids
galactose - beta -1 -4- glucose
optical activity
46. 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
unsaturated fatty acid
alpha helix
stereoisomers
antiparallel beta sheet
47. Histidine
glucose - beta -1 -4- glucose
glycerol
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
2 things about the cyclic form of a sugar as an acetal
48. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
amphoteric
C3H6O3 - with one chiral center
pyranose
will have pI of 6
49. Unique feature of glycine
secondary structure
L- amino acid
glycogen
only achiral amino acid
50. Characteristics of hydrophobic amino acids
unsaturated fatty acid
Cause of Amino acid separation in gel electrophoresis
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
primary structure