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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. 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
1. presence of strong acids 2. proteolytic enzymes
alpha helix
glutamic acid and aspartic acid
histidine - arginine - lysine
2. Amino group placed on the left of a fischer projection is a?
L- amino acid
Beta pleated sheet
NH2CONH2
have an R group that is polar enough to H bond - but does no acts an acid or a base
3. Naturally occurring carbohydrates are formed from what?
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
CH3COOH
D- glyceraldehyde
modulates fluidity and seeks to maintain optimal fluidity
4. Physiological pH
7.4
stereoisomers
ketose
modulates fluidity and seeks to maintain optimal fluidity
5. 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
packing and energy content
anomeric carbon
peptide bond
glucose - alpha -1 -2- fructose
6. What describes the affinity of functional groups for a proton?
pyranose
unsaturated fatty acid
1. presence of strong acids 2. proteolytic enzymes
Ka
7. Fatty acid structure
maltase
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
mutarotation
8. 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)
furanose
quaternary structure
have amino group in their side chains
only achiral amino acid
9. Characteristics of acidic amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
L- amino acid
glycogen
mutarotation
10. Glycosidic linkage of sucrose
all acidic - basic - and polar amino acids
unsaturated fatty acid
amphipathic
glucose - alpha -1 -2- fructose
11. Hydrophilic amino acids
only amino acid that his a secondary amine
all acidic - basic - and polar amino acids
D- amino acid
serine - threonine - asparagine - glutamine - cysteine - tyrosine
12. Enzymes that hydrolyze fats
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
7.4
lipases
furanose
13. 2 covalent bonds formed in proteins
D- amino acid
glucose - beta -1 -4- glucose
serine - threonine - asparagine - glutamine - cysteine - tyrosine
peptide bonds and disulfide bonds
14. Macromolecule that performs a variety of bodily functions and is composed of up to 20 different amino acids
D- glyceraldehyde
cysteine and methionine
Proteins
will have pI of 6
15. Fatty acid w/ no double bonds and maximum number of hydrogens
saturated fatty acid
glucose - alpha -1 -4- glucose
optical activity
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
16. Glycosidic linkage of maltose
glutamic acid and aspartic acid
3 things about the cyclic form of a sugar as a hemiacetal
glucose - alpha -1 -4- glucose
maltase
17. Fxn of cholesterol in the membrane?
modulates fluidity and seeks to maintain optimal fluidity
amphoteric
packing and energy content
mutarotation
18. Characteristics of polar amino acids
will have pI of 6
addition of water across of a bond
tertiary structure
have an R group that is polar enough to H bond - but does no acts an acid or a base
19. What configuration do all naturally occuring amino acids have?
isomers
triacylglycerol
phospholipids
L- configuration
20. Molecule can act as a base and as an acid
L- amino acid
amphoteric
histidine - arginine - lysine
L- configuration
21. 2 reasons why fats have more efficient energy stores than carbs
isoelectric point
packing and energy content
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
peptide bonds and disulfide bonds
22. Energy storage molecule of carbohydrates for animals
glucose - alpha -1 -2- fructose
lactase
glycogen
cysteine and methionine
23. Epimers of sugars that vary in the configuration of their anomeric carbons
L- amino acid
1. presence of strong acids 2. proteolytic enzymes
anomers
D- glyceraldehyde
24. Diastereomers that vary in the configuration of 1 chiral center
epimers
isomers
all acidic - basic - and polar amino acids
secondary structure
25. Energy storage molecule of carbohydrates for plants
disulfide bond
ketose
packing and energy content
starch
26. D and L describe what?
have acidic carboxylic acid on side chains - w/ pKa around 4
starch
lipases
the basic precursor of the molecule (L or D glyceraldehyde)
27. Sugar with an aldehyde at the first carbon position
C3H6O3 - with one chiral center
saturated fatty acid
2 things about the cyclic form of a sugar as an acetal
aldose
28. Glycosidic linkage of cellulose
lipases
phospholipids
glucose - beta -1 -4- glucose
ketose
29. Polar amino acids
glucose - alpha -1 -4- glucose
parallel beta sheet
glucose - beta -1 -4- glucose
serine - threonine - asparagine - glutamine - cysteine - tyrosine
30. Structure where H bonds occur btw residues distant from each other - or on a separate chain. backbone is extended rather than coiled
has thiol group that allows it the form disulfide bond
only amino acid that his a secondary amine
primary structure
Beta pleated sheet
31. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
serine - threonine - asparagine - glutamine - cysteine - tyrosine
glycerol
stereoisomers
modulates fluidity and seeks to maintain optimal fluidity
32. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
anomeric carbon
lactase
Cause of Amino acid separation in gel electrophoresis
CH3COOH
33. What stabilizes lipid bilayer?
glycerol
van der Waal forces of hydrophobic tails
the basic precursor of the molecule (L or D glyceraldehyde)
CH3COOH
34. PH at which the amino acid has a net neutral charge
alpha helix
tertiary structure
van der Waal forces of hydrophobic tails
isoelectric point
35. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
antiparallel beta sheet
L- configuration
has thiol group that allows it the form disulfide bond
anomeric carbon
36. Unique feature of glycine
only achiral amino acid
epimers
quaternary structure
D- glyceraldehyde
37. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
epimers
ketose
tertiary structure
D- glyceraldehyde
38. The amino acid sequence of a protein that is determined by peptide bond
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
histidine - arginine - lysine
ketose
primary structure
39. 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
the basic precursor of the molecule (L or D glyceraldehyde)
aldose
3 things about the cyclic form of a sugar as a hemiacetal
have an R group that is polar enough to H bond - but does no acts an acid or a base
40. Glycosidic linkage of lactose
histidine - arginine - lysine
addition of water across of a bond
alpha helix
galactose - beta -1 -4- glucose
41. Nonpolar - hydrophobic amino acids
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
glucose - beta -1 -4- glucose
only amino acid that his a secondary amine
7.4
42. PH at which positive and negative charges balance to form a zwitterion
all acidic - basic - and polar amino acids
aldose
pI
secondary structure
43. Name for 6 membered ring
3 things about the cyclic form of a sugar as a hemiacetal
lipases
addition of water across of a bond
pyranose
44. Histidine
D- glyceraldehyde
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
Proteins
glutamic acid and aspartic acid
45. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
starch
will have pI of 6
lipases
maltase
46. Enzyme that hydrolyzes lactose into galactose and glucose into
lactase
modulates fluidity and seeks to maintain optimal fluidity
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
quaternary structure
47. Hydrolysis
addition of water across of a bond
pI
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
starch
48. Glyceraldehyde
NH2CONH2
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
optical activity
C3H6O3 - with one chiral center
49. 4 causes of denaturation of proteins
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
glycerol
C3H6O3 - with one chiral center
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
50. Fatty acid w/ one or more double bonds in cis form predominately
amphoteric
unsaturated fatty acid
Ka
alpha helix