This is a very simpllistic approach to protein folding, which ignores solvent and volume effects, but it allows us to practice what we have learned about thermodynamics and kinetics. Enzymes are long chains of amino acids that have to fold in the proper way so as to exhibit enzyme activity. They can catalyze certain reactions. Let us pick a reaction in the human body at 37 C, we will call it enzyme X.

Let's say that enzyme X is the catalyst responsible for breaking starch down to individual glucose molecules. What of the following things can happen to the starch and enzyme system if you rainse the temperature?

a-the rate of the reaction of starch going to glucose will increase

b-nothing should happen since a catalyst does not affect the equilibrium

c-the enzyme could stop working effectively becauset the folded form would stop being made and would start to unravel if the process is reversible

d-the equilibrium constant will get bigger to favor the glucose side more

I can ferment glucose and can grow in anaerobic environment via fermentation of this sugar. I also produce purple color in a microbiological test to which oil is added to stimulate the formation of anaerobic environment.

1. What is the substrate of the enzyme, the presence or absence of which will determine whether the test, with the purple color, will be positive or negative

a) glucose            b) amino acid(s)               c) protein                      d) lipids

2. What is the indicator of the test media from question 13.

a) amylase    b) methyl green    c) ferric ammonium citrate    d) bromcresol purple     e) iron

3. What is the nature of the chemical reaction catalyzed by this enzyme?

a) hydrolysis of nucleotides                                   b) hydrolysis of proteins

c) decarboxylation of amino acids                        d) deamination of amino acids

I can not grow in a viscous environment. I don’t have DNAse.

4. What will be the color of the growth around me, if I lack these skills?

a) colorless       b) green              c) red                      d) black

5. I can remove amine groups from amino acids such as phenylalanine. What will be the color associated with my growth after the addition of the appropriate indicator?

a) colorless                b) green               c) red                           d) black

6. I am a test where no indicator is needed. I am whitish in color to begin with and when bacteria that grows on me makes the right enzyme, you could see a halo around its growth. What is my name?

a) lipase test                 b) Glucoronate test                 c) amylase test                         d) casease test

Describe (i) how the process of molecular evolution generates protein

families, and (ii) how the amino acid sequence alignments based on sequence similarities for such

members of a protein family can be used to identify conserved regions of a protein and construct a

phylogenetic tree of such members of a protein family. (iii) Will amino acids at the active site of an

enzyme tend to be conserved in a protein family? Why?

Japanese researchers examined mutant alleles of a gene that encodes an enzyme, liver-type arginase, in four patients. The normal protein catalyzes the breakdown of the amino acid arginine. In argininemia, lack of the enzyme causes progressive developmental disabilities, spastic limb movements, seizures and stunted growth.

The mRNA transcript for this gene codes for 322 amino acids, but the entire gene is 11.5 kilobases long, and is located on chromosome 6q. Argininemia affects both sexes and is inherited from carrier parents.

Patient A – homozygous for a G mutated to an A at DNA base 365 in the gene

Patient B – homozygous for a G to C mutation at base 703, which substitutes one amino acid for another.

Patient C – has patient A’s mutation and patient’s B mutation.  

Patient D – has patient’s A mutation in one allele, and the other allele is a deletion of a C at position 842.

The researchers evaluated the phenotype associated with each allele by producing the encoded proteins in E. coli cells. Patient A’s abnormal protein is too short. The other mutations yield proteins of normal length that are unstable or otherwise nonfunctional.

1. The mode of inheritance of argininemia is ___________________________________________

2. Patients _____ and ______ are heterozygous for the argininemia gene.

3. Patients ____ and _____have missense mutations for the argininemia gene.

4. Why is patient A’s liver-type arginase too short?

5. Human liver-type arginase can be produces in E. coli because: A) E. coli have livers B) The genetic code is universal C) The genetic code is triplet D) E. coli also uses arginine

6. The argininemia gene has enough bases beyond those in exons to encode ____________more amino acids.

suggest how a protein might have been hydrolyzed to give the amino acids. keep in mind that this is made from human consumption.

QUESTION 73

Gluconeogeneis is _________________.

QUESTION 72

Electrons extracted from fatty acids in the peroxisomes are transferred to __________________.

QUESTION 65

What type of enzyme is required to catabolize an unsaturated fatty acid but not a saturated fatty acid?

multi answer may apply

please answer all the question

A human hemoglobin variant occurs in certain populations. The variant hemoglobin is slightly defective in its oxygen carrying function, causing a mild anemia. Normal alpha-hemoglobin has 141 amino acids, while the variant α-polypeptide is 150 amino acids long.

Beginning with the final amino acid coding codon (CGU Arg) the 3' region of the normal α-globin mRNA has the sequence:

5’ ...CGU UAA CCU UCG GUA GCA UGU GAU CCU CAC UAG GCC UCC GGG... 3’

a) Based on this information, explain how the variant α-hemoglobin is likely generated.

b) What is the sequence of the four C terminal amino acids of the variant α-hemoglobin.

An enzyme normally functions at pH 4. At pH 8, it is denatured. How can a change in pH cause denaturation in a protein composed of more than one polypeptide? The change in hydrogen ion concentration can affect enzyme structure and function by __________.

A 3000 bp region of the human genome encodes two genes. One of the genes encodes a protein of 700 amino acids and the other gene encodes a protein of 310 amino acids. The mRNA sequences of the two genes do not contain any of the same nucleotide sequences. How is this possible?

That's all the information given. I think I'm supposed to mention terms like "reading frame" but this question doesn't make any sense