ANATOMY 2300.01 Study Guide - Midterm Guide: Lean Body Mass, Calcium Metabolism, Low-Density Lipoprotein

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harlequinprairie-dog105

5 Oct 2018

School

Ohio State University

Department

Anatomy

Course

ANATOMY 2300.01

Professor

All

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Document Summary

Form important structures in body, make up key part of blood, help regulate body functions, can fuel body cells. Functions: regulates and maintains body functions, provides essential form of nitrogen (in the dorm of amino acids) Protein is long strand of amino acids linked by a covalent bond (sequence determines function) 20 different amino acids make up all proteins. 9 essential amino acids (needed by the body because it"s (cid:374)ot produ(cid:272)ed i(cid:374) the (cid:271)od(cid:455)(cid:895) The r group differs in all amino acids. Can be used by muscle for energy needs. Whey protein (from milk) is a rich source of bcaas- other benefits (carbs, calcium, electrolytes) Essential amino acids- cannot be synthesized by humans in sufficient amounts or at all, must be included in diet. Limiting amino acids- essential amino acid in lowest concentration in food or diet relative to body needs (limits what the body can do)

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Instructions

BACKGROUND

The amino acid sequence for a protein that is associated with the onset of Huntington's Disease in humans is 582 amino acids long and is provided below. This disease is autosomal dominant and results in a prolonged degeneration of nerve cells in the brain.

INSTRUCTIONS

For this assignment, use any method you determine most feasible (i.e. programming in MATlab, R script, Crystal Ball, Witchcraft/Hocus Pocus, etc.) to decipher the amino acid composition of this protein and answer the 15 questions associated with this protein and its associated amino acid structure.

You will be calculating proportions (percentages - %) for this assignment. Calculate all proportions to 1 decimal place and make sure you have rounded up or down correctly. If unsure, use a spreadsheet program such as Excel to display your proportional calculations to 1 decimal place.

Spelling matters (Incorrect spelling will be graded as such - incorrect).

Huntington Disease Associated Protein Amino Acid Sequence

The first amino acid below ('m') represents the amino (NH3) terminus of this protein. The last amino acid in this sequence represents the carboxy (COOH) terminus and is the very last 'c' at the bottom of this protein sequence structure. The amino acids are numbered individually across the rows (left to right) beginning from the amino terminus (#1) to the carboxy terminus (#582).

mvskreniat	hhlyqawdpv	pslspattga	lisheklllq	inperelgsm	syklgqvsih
svwlgnsitp	lreeewdeee	eeeadapaps	spptspvnsr	khragvdihs	csqfllelys
rwilpsssar	rtpailisev	vrsllvvsdl	fternqfelm	yvtltelrrv	hpsedeilaq
ylvpatckaa	avlgmdkava	epvsrllest	lrsshlpsrv	galhgilyvl	ecdllddtak
qlipvisdyl	lsnlkgiahc	vnihsqqhvl	vmcatafyli	enypldvgpe	fsasiiqmcg
vmlsgseest	psiiyhcalr	glerlllseq	lsrldaeslv	klsvdrvnvh	sphramaalg
lmltcmytgk	ekvspgrtsd	pnpaapdses	vivamervsv	lfdrirkgfp	cearvvaril
pqflddffpp	qdimnkvige	flsnqqpypq	fmatvvykvf	qtlhstgqss	mvrdwvmlsl
snftqrapva	matwslscff	vsastspwva	ailphvisrm	gkleqvdvnl	fclvatdfyr
hqieeeldrr	afqsvlevva	apgspyhrll	tclrnvhkvt	tc	CARBOXY TERMINUS

I need these decoded in order to answer the following questions:

a.) What is the name of the least abundant amino acid in this protein and what proportion of the total amino acids in the protein does this individual amino acid represent?

b.) What is the proportion of essential amino acids included in this protein sequence?

c.)How many Tryptophan residues are present in this protein sequence?

d.) The amino acid sequence from residues 73-85 is represented by the amino acids EEEWDEEEEEEAD, how would you generally classify this small region of the protein

e.) Two amino acids are present in the same proportion in this protein, which two are those?

f.) How many positively charged amino acids are present in this protein?

g.)Which class of amino acids is the most abundant in this protein?

h.) What amino acid(s) is/are present at locations 572 and 582 in the Huntington Disease protein (Full Amino Acid Name(s))

i.) What type of structure could form between these amino acids that could help stabilize this protein's structure?

j.) How many valine residues are present in this protein?

k.)Which class of amino acids is least abundant in this protein?

l.) How may negatively charged amino acids are present in the Huntington disease protein?

m.) How many Aspartic Acid residues are present in this protein and what proportion do they represent of the total amino acids in this protein?

n.)Summed together, how many hydrophilic amino acid residues are present in this protein?

o.)What is the sequence of amino acids from positions 487-492 (First letters only)?

p.) How would you classify this area of the Huntington protein based on these amino acids?

Question 9

Codominance is a form of inheritance in which two different allelesfor a gene are both expressed, and neither allele is dominant overthe other. One example of codominance is fur color in cattle; thealleles for red fur and white fur are codominant. If a homozygousred cow and a homozygous white bull mate, what would you expect tofind in their offspring?.912.l.16.2>

They will all have white fur.

Their fur will be a mixture of red and white hairs.

Their fur will be a lighter shade of red.

They will all have red fur.

Question 10

If a tRNA molecule has an anticodon which reads AUG, what will itmatch up with and what amino acid is it carrying?
.912.l.16.5>

	U		C		A		G
	UUU	Phenylalanine	UCU	Serine	UAU	Tyrosine	UGU	Cysteine	U
U	UUC	Phenylalanine	UCC	Serine	UAC	Tyrosine	UGC	Cysteine	C
	UUA	Leucine	UCA	Serine	UAA	Stop	UGA	Stop	A
	UUG	Leucine	UCG	Serine	UAG	Stop	UGG	Tryptophan	G
	CUU	Leucine	CCU	Proline	CAU	Hisitidine	CGU	Arginine	U
C	CUC	Leucine	CCC	Proline	CAC	Hisitidine	CGC	Arginine	C
	CUA	Leucine	CCA	Proline	CAA	Glutamine	CGA	Arginine	A
	CUG	Leucine	CCG	Proline	CAG	Glutamine	CGG	Arginine	G
	AUU	Isoleucine	ACU	Threonine	AAU	Asparagine	AGU	Serine	U
A	AUC	Isoleucine	ACC	Threonine	AAC	Asparagine	AGC	Serine	C
	AUA	Isoleucine	ACA	Threonine	AAA	Lysine	AGA	Arginine	A
	AUG	Methionine/Start	ACG	Threonine	AAG	Lysine	AGG	Arginine	G
	GUU	Valine	GCU	Alanine	GAU	Aspartate	GGU	Glycine	U
G	GUC	Valine	GCC	Alanine	GAC	Aspartate	GGC	Glycine	C
	GUA	Valine	GCA	Alanine	GAA	Glutamate	GGA	Glycine	A
	GUG	Valine	GCG	Alanine	GAG	Glutamate	GGG	Glycine	G

It is carrying arginine and will match with a CGU codon on themRNA.

It is carrying methionine and will match with a TAC codon on theDNA.

It is carrying methionine and will match with a UAC codon on themRNA.

It is carrying tyrosine and will match with a UAC codon on themRNA.

Question 11

While the DNA in a human skin cell was being replicated, a singlebase was miscopied. What will be the most likely result of this forthe cell in which it happened?.912.l.16.3>

All the proteins the cell creates from the miscopied strand willdo different jobs than the old ones.

If the new sequence codes for the same amino acid as theoriginal cell, it will function normally.

Both new DNA strands will end up together in a new cell, and theinaccurate one will be discarded.

Any miscopied DNA will be replaced with an accurate DNA copyonce the cell divides.

Question 12

A ferret's haploid number of chromosomes is 20. How would thenumber of chromosomes in the ferret's body cells compare to thenumber of chromosomes in its gametes?.912.l.16.17>

Its body cells would have 20 chromosomes, and its gametes wouldhave 40 chromosomes.

Its body cells and gametes would both have 40 chromosomes.

Its body cells and gametes would both have 20 chromosomes.

Its body cells would have 40 chromosomes, and its gametes wouldhave 20 chromosomes.

Question 13

A body cell is in the longest stage of its life cycle. The cellgrows, synthesizing proteins and increasing in size. Eventually,the cell will grow too large to carry out normal activities. Whichof the following is the best conclusion you can make about the lifecycle of this cell?.912.l.16.14>

The cell is close to the end of its life cycle, and a chemicalsignal will initiate cell death.

The cell is ready to undergo mitosis, and a chemical signal willsend the cell to prophase.

The cell is in the G1 phase of interphase, and a chemical signalwill send the cell to the S phase.

The cell is in the S phase of interphase, and a chemical signalwill move the cell to the G2 phase.

Question 14

While mRNA strands are being created a sequence is sometimesmiscopied. What is the best possible outcome for the cell shouldthis take place?.912.l.16.5>

The miscopied sequence codes for the same amino acids as theoriginal sequence.

The new sequence creates a protein that serves a differentfunction from the original.

The ribosomes will correct the mistake before the tRNA matchesan amino acid to it.

The mRNA will only be used to create non-critical proteins forthe cell.

Question 15

Over the last several decades, the scientific community hasgathered a large amount of information regarding genetics andgenetic variation. What are two main sources that lead toincreased genetic variation?.912.l.15.15>

Selective breeding

Gamete mutations

Recombination

Genetic drift

salmonlouse680

Biochemistry Review Questions

What is the classification of the compound shown here?

A) an aldohexose B) a ketohexose C) an aldopentose D) a ketopentose

2. In a disaccharide, the CâO bond that joins the two rings together is called _____.

A) a hemiacetal B) a glycosidic linkage C) an alditol D) an anomer

3. What is the structure of amylopectin?

A) unbranched skeleton of glucose molecules joined by 1ï®4-ï¡-glycoside linkages

B) branched skeleton of glucose molecules joined by 1ï®4-ï¡-glycoside linkages

C) unbranched skeleton of glucose molecules joined by 1ï®4-ï¢-glycoside linkages

D) branched skeleton of glucose molecules joined by 1ï®4-ï¢-glycoside linkages

4. In a disaccharide, the CâO bond that joins the two rings together is called _____.

A) a hemiacetal B) a glycosidic linkage C) an alditol D) an anomer

5. Which type of linkage between the two rings is in the structure shown?

A) 1Â®4-b-glycoside linkage D) 1Â®1-a-glycoside linkage

B) 1Â®4-a-glycoside linkage E) 1Â®2-b-glycoside linkage

C) 1Â®1-b-glycoside linkage

6. What is the structure of cellulose?

A) unbranched skeleton of glucose molecules joined by 1Â®4-a-glycoside linkages

B) branched skeleton of glucose molecules joined by 1Â®4-a-glycoside linkages

C) unbranched skeleton of glucose molecules joined by 1Â®4-b-glycoside linkages

D) branched skeleton of glucose molecules joined by 1Â®4-b-glycoside linkages

7. Which amino acid is a basic amino acid?

A) serine B) arginine C) cysteine D) alanine E) valine

8. What monosaccharide is found in cellulose, starch, and glycogen?

A) glucose

B) galactose

C) N-acetyl-D-glucosamine

D) fructose

E) More than one of the monosaccharides above is found in cellulose, starch, and glycogen.

9. Which is not a reducing sugar?

A) glucose B) fructose C) sucrose D) galactose E) an aldopentose

10. Sucrose contains one _____ unit and one _____ unit.

11. What is the particular sequence of amino acids of a protein that are joined together by peptide bonds called?

A) the primary structure of a protein C) the tertiary structure of a protein

B) the secondary structure of a protein D) the quaternary structure of a protein

12. What is the charge on an amino acid at a pH below its pI?

A) positive

B) neutral

C) negative

D) The charge or lack of charge varies depending on the amino acid.

13. What is the C-terminal amino acid in the tetrapeptide glycylalanyisoleucylmethionine?

A) alanine B) glycine C) methionine D) isoleucine

14. How many different dipeptides can be formed when one valine reacts with one glycine?

A) 1 B) 2 C) 3 D) 4

15. What is the process of altering the shape of a protein without breaking the amide bonds that form the primary structure?

A) hydrolysis B) competitive inhibition C) denaturation D) oxidation

16. Which of the following compounds is an enzyme?

A) glucose C) N-acetyl-D-glucosamine

B) triosephosphate isomerase D) dihydrofolate

17. What is a zymogen?

A) an amino acid with a neutral charge

B) inactive precursor of an enzyme

C) a molecule that causes an enzyme to lose activity

D) a nonprotein organic molecule needed for an enzyme-catalyzed reaction to occur

18. Which of the following will the cause the rate of enzyme activity to first increase and then level off?

increasing the enzyme concentration

increasing the temperature

increasing the substrate concentration

increasing the pH

19. Which of the following make up a nucleoside?

base + sugar

base + phosphate + sugar

base + phosphate

phosphate + sugar

20. Transcription corresponds to which of the following?

the separation of the two strands of DNA to enable the formation of two identical DNA molecules

the transfer of genetic information from DNA to RNA

the transfer of genetic information from RNA to DNA

the use of genetic information to synthesize a specific protein

21. Each individual tRNA contains _____

A) a base sequence that is identical to the informational strand of DNA.

B) the sequence of codons that determines the order of amino acids in the protein.

C) an anticodon of three nucleotides that is complementary to the codon in mRNA and identifies individual amino acids.

D) an anticodon complementary to any of the three stop codons.

22. Where does energy production occur in animal cells?

A) cell membrane B) cytoplasm C) mitochondria D) nucleus

23. How many molecules of CO2 are produced for each turn of the citric acid cycle?

A) 0 B) 1 C) 2 D) 3 E) 4

25. Which is not a reaction found in stage [2] of catabolism?

A) fatty acid oxidation C) oxidative phosphorylation

B) glycolysis D) amino acid catabolism

26. What is the classification of the reaction shown?

A) oxidation D) hydrolysis

B) reduction E) isomerization

C) decarboxylation

27. Synthesis of glucose from amino acids is called

A) Glycolysis C) Gluconeogensis

B) Glycogenesis D) Hydrolysis

28. The synthesis of large molecules from smaller ones in the body is referred to as

A) catabolism C) Ketogenesis

B) anabolism D)glycolysis

29. The nucleic acid base found in the mRNA but not in DNA is

A) Adenine C) Uracil

B) Guanine D) Cytosine

30. DNA rich in A-T base pairs have

A) 1 hydrogen bond C) 2 hydrogen bonds

B) 3 hydrogen bonds D) 4 hydrogen bonds

31. Where does the energy production occur in the cell?

A) Ribosome C) Mitochondria

B) Nucleus D) Cytoplasm

32. Where does the protein synthesis occur in the cell?

A) Ribosome C) Mitochondria

B) Nucleus D) Cytoplasm

33. In the process of transcription, the flow of genetic information is from

A) DNA to DNA C) DNA to protein

B) RNA to protein D) DNA to RNA

34. Ammonium ions are converted to non-toxic nitrogen containing compounds through

A) Amino acid metabolism C) Urea cycle

B) Citric acid cycle D) transamination

35. In protein structure, B-pleated cheats are examples of

A) Primary structure C) Secondary structure

B) Tertiary structure D) Quaternary structure

36. Lactose is a disaccharide formed of

A) Glucose + fructose C) Glucose + galactose

B) Glucose + glucose D) Fructose + galactose

37. Saponification is

A) Hydrolysis of fats by strong base

B) Hydrolysis of glycerol by lipases

C) Esterification

D) Oxidation reaction

38. The connection between amino acid residues in molecules of protein is

A) glycosidic linkage C) peptide linakge

C) ether linkage D) phosphodiester linkage

39. Polyunsaturated fatty acids are generally

A) Oil at room temperature C) Solid at room temperature

B) Semisolid at room temperature D) All of the above

40. Maximum energy is produced by

A) Carbohydrates C) Lipids

B) Proteins D) Nucleic acids

41. A polynucleotide contains _____

A) one free phosphate group at the 5' end.

B) a backbone of alternating sugar and base groups.

C) one free phosphate group at the 1' end.

D) one free OH group at the 5' end.

42. How many molecules of CO2 are produced for each turn of the citric acid cycle?

A) 0 B) 1 C) 2 D) 3 E) 4

43. How many molecules of GTP are produced for each turn of the citric acid cycle?

A) 0 B) 1 C) 2 D) 3 E) 4

44. Which is the enzyme that hydrolyzes triacylglycerols?

A) acetyl CoA D) lipase

B) protease pepsin E) succinate dehydrogenase

C) amylase

ANATOMY 2300.01 Study Guide - Midterm Guide: Lean Body Mass, Calcium Metabolism, Low-Density Lipoprotein

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