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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. Unique feature of proline
disulfide bond
lipases
epimers
only amino acid that his a secondary amine
2. Characteristics of polar amino acids
isoelectric point
have an R group that is polar enough to H bond - but does no acts an acid or a base
cysteine and methionine
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
3. Unique feature of glycine
cysteine and methionine
only achiral amino acid
Cause of Amino acid separation in gel electrophoresis
glycerol
4. 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
7.4
alpha helix
the basic precursor of the molecule (L or D glyceraldehyde)
only amino acid that his a secondary amine
5. Glycosidic linkage of lactose
D- glyceraldehyde
peptide bond
glycogen
galactose - beta -1 -4- glucose
6. PH at which the amino acid has a net neutral charge
Characteristics of the peptide bond
has thiol group that allows it the form disulfide bond
isoelectric point
CH3COOH
7. Separation is due to charge - with negative charge moving toward positive electrode and positive charge moving toward negative electrode
have amino group in their side chains
amphipathic
optical activity
Cause of Amino acid separation in gel electrophoresis
8. (R) and (S) describe what?
secondary structure
C3H6O3 - with one chiral center
absolute configuration
only amino acid that his a secondary amine
9. What configuration do all naturally occuring amino acids have?
glucose - alpha -1 -2- fructose
parallel beta sheet
the basic precursor of the molecule (L or D glyceraldehyde)
L- configuration
10. Name for 5 membered ring
quaternary structure
alpha helix
disulfide bond
furanose
11. Name for 6 membered ring
pyranose
glycogen
parallel beta sheet
D- amino acid
12. Characteristics of acidic amino acids
have acidic carboxylic acid on side chains - w/ pKa around 4
aldose
triacylglycerol
have an R group that is polar enough to H bond - but does no acts an acid or a base
13. Fatty acid w/ no double bonds and maximum number of hydrogens
Cause of Amino acid separation in gel electrophoresis
anomers
saturated fatty acid
glutamic acid and aspartic acid
14. Sulfur containing amino acids
disulfide bond
cysteine and methionine
anomeric carbon
pI
15. 2 reasons why fats have more efficient energy stores than carbs
secondary structure
have an R group that is polar enough to H bond - but does no acts an acid or a base
packing and energy content
furanose
16. Fatty acid w/ one or more double bonds in cis form predominately
glucose - alpha -1 -4- glucose
glutamic acid and aspartic acid
will have pI of 6
unsaturated fatty acid
17. Epimers of sugars that vary in the configuration of their anomeric carbons
have amino group in their side chains
anomers
starch
1. presence of strong acids 2. proteolytic enzymes
18. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
parallel beta sheet
mutarotation
will have pI of 6
have an R group that is polar enough to H bond - but does no acts an acid or a base
19. 3 physiological roles of lipids
galactose - beta -1 -4- glucose
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
unsaturated fatty acid
20. D and L describe what?
the basic precursor of the molecule (L or D glyceraldehyde)
tertiary structure
mutarotation
has thiol group that allows it the form disulfide bond
21. Sugar with a carbonyl group at the 2 carbon position
have amino group in their side chains
stereoisomers
L- amino acid
ketose
22. Diastereomers that vary in the configuration of 1 chiral center
cysteine and methionine
the basic precursor of the molecule (L or D glyceraldehyde)
epimers
glucose - alpha -1 -2- fructose
23. 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)
glycogen
absolute configuration
quaternary structure
lipases
24. Initial folding of proteins into shapes stabilized by H bonds btw amino and carboxyl groups of backbone
Ka
aldose
secondary structure
maltase
25. Formula for urea
optical activity
NH2CONH2
glucose - beta -1 -4- glucose
Cause of Amino acid separation in gel electrophoresis
26. Nonpolar - hydrophobic amino acids
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
amphipathic
furanose
van der Waal forces of hydrophobic tails
27. 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 urea 2. extreme pH 3. extreme temperature 4. changes in salinity
peptide bond
have an R group that is polar enough to H bond - but does no acts an acid or a base
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
28. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
isoelectric point
ketose
1. presence of strong acids 2. proteolytic enzymes
will have pI of 6
29. Energy storage molecule of carbohydrates for animals
addition of water across of a bond
glycogen
maltase
peptide bonds and disulfide bonds
30. 2 covalent bonds formed in proteins
packing and energy content
L- amino acid
serine - threonine - asparagine - glutamine - cysteine - tyrosine
peptide bonds and disulfide bonds
31. Interconversion btw two anomers
glucose - alpha -1 -4- glucose
mutarotation
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
starch
32. Generated btw either thiols on different proteins or thiols on the same protein
glycogen
disulfide bond
3 things about the cyclic form of a sugar as a hemiacetal
glutamic acid and aspartic acid
33. 2 things that accelerate the rate of hydrolysis for peptide cleavage?
1. presence of strong acids 2. proteolytic enzymes
all acidic - basic - and polar amino acids
peptide bond
anomers
34. PH at which positive and negative charges balance to form a zwitterion
modulates fluidity and seeks to maintain optimal fluidity
1. presence of strong acids 2. proteolytic enzymes
glycerol
pI
35. Storage form of fatty acid that is composed of 3 esterified fatty acid to a glycerol molecule
glucose - beta -1 -4- glucose
triacylglycerol
quaternary structure
furanose
36. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
2 things about the cyclic form of a sugar as an acetal
1. presence of strong acids 2. proteolytic enzymes
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
anomeric carbon
37. Enzyme that hydrolyzes maltose into 2 glucose molecules?
peptide bonds and disulfide bonds
pI
maltase
packing and energy content
38. Property of fatty acids where one end is hydrophobic and the other is hydrophilic
pI
disulfide bond
pyranose
amphipathic
39. Glycosidic linkage of maltose
quaternary structure
glucose - alpha -1 -4- glucose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
pyranose
40. (+) and (-) describe what?
optical activity
epimers
anomeric carbon
maltase
41. Molecules with the same atoms - but different bonds
saturated fatty acid
quaternary structure
isomers
peptide bond
42. Basic amino acids
histidine - arginine - lysine
L- amino acid
triacylglycerol
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
43. The amino acid sequence of a protein that is determined by peptide bond
glucose - beta -1 -4- glucose
primary structure
have amino group in their side chains
1. presence of strong acids 2. proteolytic enzymes
44. Naturally occurring carbohydrates are formed from what?
isomers
galactose - beta -1 -4- glucose
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
D- glyceraldehyde
45. Enzyme that hydrolyzes lactose into galactose and glucose into
lactase
triacylglycerol
L- configuration
Cause of Amino acid separation in gel electrophoresis
46. Energy storage molecule of carbohydrates for plants
starch
antiparallel beta sheet
unsaturated fatty acid
glucose - alpha -1 -2- fructose
47. 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
amphipathic
anomeric carbon
D- glyceraldehyde
48. Adjacent polypeptide strands running in opposite directions in Beta pleated sheet structure
quaternary structure
have amino group in their side chains
Characteristics of the peptide bond
antiparallel beta sheet
49. 1.has partial double bond character due to resonance 2. it cannot rotate 3. amide H is someWhat acidic and can H bond
lactase
cysteine and methionine
Characteristics of the peptide bond
7.4
50. Fatty acid structure
2 things about the cyclic form of a sugar as an acetal
peptide bonds and disulfide bonds
glycerol
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic