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