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