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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
amphipathic
alpha helix
glycerol
modulates fluidity and seeks to maintain optimal fluidity
2. Glycosidic linkage of maltose
1. presence of strong acids 2. proteolytic enzymes
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
glucose - alpha -1 -4- glucose
3. Unique feature of cysteine
CH3COOH
aldose
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
has thiol group that allows it the form disulfide bond
4. What configuration do all naturally occuring amino acids have?
unsaturated fatty acid
C3H6O3 - with one chiral center
L- configuration
Cause of Amino acid separation in gel electrophoresis
5. Hydrophobic and hydrophilic interactions btw amino acids more distant from each other on the polypeptide chain
unsaturated fatty acid
tertiary structure
triacylglycerol
NH2CONH2
6. Enzymes that hydrolyze fats
glucose - alpha -1 -2- fructose
lipases
pI
van der Waal forces of hydrophobic tails
7. Polar amino acids
serine - threonine - asparagine - glutamine - cysteine - tyrosine
glucose - alpha -1 -4- glucose
starch
anomeric carbon
8. Name for 5 membered ring
furanose
starch
pyranose
maltase
9. Diastereomers that vary in the configuration of 1 chiral center
primary structure
secondary structure
epimers
peptide bonds and disulfide bonds
10. Amino group placed on the right of a fischer projection is a?
anomers
D- amino acid
tertiary structure
starch
11. 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
triacylglycerol
only achiral amino acid
3 things about the cyclic form of a sugar as a hemiacetal
peptide bond
12. Unique feature of proline
only amino acid that his a secondary amine
have acidic carboxylic acid on side chains - w/ pKa around 4
glycogen
saturated fatty acid
13. Characteristics of hydrophobic amino acids
have alkyl or aromatic side chains and tend to associate w/ each other - rather than water
will have pI of 6
glucose - beta -1 -4- glucose
peptide bond
14. 2 reasons why fats have more efficient energy stores than carbs
tertiary structure
will have pI of 6
packing and energy content
anomeric carbon
15. 1. it requires an enzyme to linearize and mutarotate 2. it is not a reducing sugar and give negative Benedict's test
7.4
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
only amino acid that his a secondary amine
2 things about the cyclic form of a sugar as an acetal
16. Interconversion btw two anomers
Beta pleated sheet
amphoteric
L- amino acid
mutarotation
17. Glycosidic linkage of cellulose
Characteristics of the peptide bond
glutamic acid and aspartic acid
serine - threonine - asparagine - glutamine - cysteine - tyrosine
glucose - beta -1 -4- glucose
18. 3 physiological roles of lipids
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
will have pI of 6
only achiral amino acid
histidine - arginine - lysine
19. Basic amino acids
secondary structure
L- amino acid
cysteine and methionine
histidine - arginine - lysine
20. (+) and (-) describe what?
serine - threonine - asparagine - glutamine - cysteine - tyrosine
optical activity
Characteristics of the peptide bond
epimers
21. The amino acid sequence of a protein that is determined by peptide bond
have an R group that is polar enough to H bond - but does no acts an acid or a base
cysteine and methionine
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
primary structure
22. 4 causes of denaturation of proteins
modulates fluidity and seeks to maintain optimal fluidity
2 things about the cyclic form of a sugar as an acetal
serine - threonine - asparagine - glutamine - cysteine - tyrosine
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
23. Carbon that in linear form has a carbonyl - or in cyclic form has a hemiacetal or an acetal
L- configuration
anomers
have amino group in their side chains
anomeric carbon
24. Molecules with the same atoms and same bonds - but different bond geometries; can either be enantiomers or diastereomers
1. presence of strong acids 2. proteolytic enzymes
histidine - arginine - lysine
stereoisomers
peptide bond
25. Fatty acid w/ one or more double bonds in cis form predominately
only amino acid that his a secondary amine
glutamic acid and aspartic acid
epimers
unsaturated fatty acid
26. 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
ketose
isomers
has thiol group that allows it the form disulfide bond
27. Acidic amino acids
glutamic acid and aspartic acid
tertiary structure
maltase
addition of water across of a bond
28. 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
D- glyceraldehyde
amphipathic
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
peptide bond
29. Sulfur containing amino acids
have amino group in their side chains
pyranose
cysteine and methionine
the basic precursor of the molecule (L or D glyceraldehyde)
30. Hydrolysis
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic
furanose
Cause of Amino acid separation in gel electrophoresis
addition of water across of a bond
31. Formula for urea
NH2CONH2
3 things about the cyclic form of a sugar as a hemiacetal
glutamic acid and aspartic acid
peptide bonds and disulfide bonds
32. Glyceraldehyde
glucose - alpha -1 -2- fructose
C3H6O3 - with one chiral center
tertiary structure
histidine - arginine - lysine
33. 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)
peptide bonds and disulfide bonds
pI
quaternary structure
Beta pleated sheet
34. Fxn of cholesterol in the membrane?
modulates fluidity and seeks to maintain optimal fluidity
isoelectric point
alpha helix
only amino acid that his a secondary amine
35. Sugar with a carbonyl group at the 2 carbon position
ketose
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
glucose - alpha -1 -2- fructose
packing and energy content
36. Rule for all amino acids that are nonbasic and nonacidic pertaining to pI value?
quaternary structure
ketose
only achiral amino acid
will have pI of 6
37. Enzyme that hydrolyzes lactose into galactose and glucose into
1. presence of urea 2. extreme pH 3. extreme temperature 4. changes in salinity
pyranose
lactase
Cause of Amino acid separation in gel electrophoresis
38. Glycosidic linkage of sucrose
isoelectric point
glucose - alpha -1 -2- fructose
will have pI of 6
pI
39. Characteristics of acidic amino acids
Characteristics of the peptide bond
Cause of Amino acid separation in gel electrophoresis
have acidic carboxylic acid on side chains - w/ pKa around 4
optical activity
40. PH at which the amino acid has a net neutral charge
van der Waal forces of hydrophobic tails
alpha helix
have an R group that is polar enough to H bond - but does no acts an acid or a base
isoelectric point
41. Energy storage molecule of carbohydrates for plants
have an R group that is polar enough to H bond - but does no acts an acid or a base
starch
have amino group in their side chains
cysteine and methionine
42. Amino group placed on the left of a fischer projection is a?
L- amino acid
glutamic acid and aspartic acid
1. presence of strong acids 2. proteolytic enzymes
Proteins
43. Acetic acid formula?
CH3COOH
parallel beta sheet
basic amino acid has pKa at 6.5 - so it can either be protonated or deprotonated at physiological pH
D- amino acid
44. Adjacent polypeptide strands running in the same direction in Beta pleated sheet structure
7.4
Beta pleated sheet
parallel beta sheet
will have pI of 6
45. PH at which positive and negative charges balance to form a zwitterion
have acidic carboxylic acid on side chains - w/ pKa around 4
1. presence of strong acids 2. proteolytic enzymes
pI
1. form phospholipids of cellular membranes 2. store energy in adipose tissue 3. produce steroid hormones
46. Unique feature of glycine
serine - threonine - asparagine - glutamine - cysteine - tyrosine
glycogen
only achiral amino acid
tertiary structure
47. Molecule can act as a base and as an acid
anomers
unsaturated fatty acid
cysteine and methionine
amphoteric
48. Glycosidic linkage of lactose
glucose - beta -1 -4- glucose
galactose - beta -1 -4- glucose
amphipathic
histidine - arginine - lysine
49. Nonpolar - hydrophobic amino acids
Beta pleated sheet
glycine - alanine - valine - methionine - leucine - isoleucine - proline - phenylalanine - tryptophan
antiparallel beta sheet
triacylglycerol
50. Fatty acid structure
maltase
D- glyceraldehyde
secondary structure
long chain of unsubstituted alkanes that end in a carboxylic acid - making them amphipathic