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