BIOLOGY 2B03 Lecture Notes - Lecture 2: Protein Kinase A, Tetrameric Protein, Metabolic Pathway

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27 Sep 2016

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3. 5 regulating protein function ii: noncovalent and covalent modifications. Noncovalent modifications usually involve the binding or dissociation of a molecule and a consequent change in the conformation of the protein. Covalent modifications include hydrolysis of the polypeptide chain or addition of a molecule to the side chain of one or more residues or to the n or c terminus of the protein. Modify the shape of the protein w/o changing the conformation of the polypeptide and its side chains ex by adding charge or bulky group. Can direct protein to particular locations in a cell. Proteolysis are irreversible can be superseded only by degradation of the modified protein and synthesis of a replacement. Noncovalent binding permits allosteric, or cooperative, regulation of proteins. Allostery change in a proteins" tertiary or quaternary structure induced by the noncovalent binding of a ligand. Regulation of protein function by conformational changes mediated through binding of an allosteric modulator.

Related Questions

Can someone please help me with the following questions.

Question 6

Proteins can be regulated by removing phosphate groups that modify specific amino acids in their sequences. This removal activity is exerted by

	a.	Protein Phosphorylases
	b.	Protein Phosphatases
	c.	Protein Kinases
	d.	Protein Phosphoproteases

Question 7

Proteolytic processing is a(n)

	a.	requirement for protein insertion into membranes
	b.	type of covalently-linked post-translational modification
	c.	irreversible post-translational modification
	d.	type of reversible post-translational modification
	e.	frequent consequence of heat denaturation

Question 8

Allosteric regulation involves

	a.	the binding of a protein to a regulatory subunit
	b.	the binding of a regulatory molecule to the active site on an enzyme
	c.	the binding of a regulatory molecule to a site on an enzyme that is distinct from the catalytic site
	d.	the binding of GTP to an enzyme to regulate its function
	e.	the binding of a Ubiquitin-like protein to an enzyme

Question 9

During N-linked glycosylation, a carbohydrate side chain is attached through a Nitrogen atom at the amino group of Serine or Threonine

True

False

Question 10

The signal sequence that targets proteins for insertion into the Endoplasmic Reticulum is rich in hydrophobic aminoacids and is most frequently located at the N-terminus of the protein

True

False

blushcamel925

QUESTION 10

If you can drink milk as an adult, it means that you have inherited a mutation in the promoter of your lactase gene (the gene that encodes the enzyme you need to break down lactose). Predict the effect of this mutation:

		The mutation changes the number of domains in the enzyme, which makes it work more efficiently
		The mutation changes the amino acid sequence of the lactase protein
		The mutation increases the number of copies of the lactase gene that will be found in your genome
		The mutation changes whether the lactase sequence is found in an intron or exon
		The mutation affects the expression of the lactase gene

1.2 points

QUESTION 11

A competitive inhibitor is decreasing the activity of an enzyme. Predict the effect of adding more substrate to the reaction.

		The substrate will increase the reaction rate by binding to the allosteric site
		The substrate will increase the reaction rate by competing with the inhibitor for the active site
		The reaction rate will not change unless the inhibitor can be removed
		The enzyme adjusts its shape so that the substrate, but NOT the competitive inhibitor, can bind
		The substrate will bind to the competitive inhibitor and block its ability to bind to the enzyme

1.2 points

QUESTION 12

What determines where in the genome a transcription regulator will bind?

		Transcription regulators bind to the 5' UTR region of a gene
		Regulators bind via complementary base-pairing to certain DNA molecules
		Covalent bonds form between the transcription regulator and the atoms of the DNA backbone
		Every eukaryotic gene has a different transcription regulator that will bind to the 5' end of the gene
		Transcription regulators bind to specific DNA sequences via multiple weak non-covalent interactions

1.2 points

QUESTION 13

What is the basic premise of cell theory?

		DNA -> RNA -> protein
		All cells arise from pre-existing cells
		DNA provides the complete instructions to create a cell
		The identity of a cell is determined through gene expression patterns
		All cells contain the same four basic macromolecules

1.2 points

QUESTION 14

What is the benefit of using BOTH the lac activator and the lac repressor to control gene expression?

		Using both an activator and repressor enables cells to more accurately determine the amount of lactose available in the environment
		Enzymes to digest lactose are only made when energy is low and lactose is available
		The activator can override the inhibition of the lac operon by the repressor
		The repressor can control the enhancer, while the activator can control the promoter
		When neither the lac activator or repressor is present, expression of the lac operon is too high

1.2 points

QUESTION 15

What is the histone code used for?

		Phosphorylation and acetylation of DNA affect its ability to be compacted
		Changes to the sequence of DNA change whether DNA will wrap around histone proteins
		Covalent modifications of histones affect the ability of the transcription initiation complex to form
		Histones provide the codon sequences needed for translation to occur
		The histone code affects which amino acids will get added to a polypeptide

BIOLOGY 2B03 Lecture Notes - Lecture 2: Protein Kinase A, Tetrameric Protein, Metabolic Pathway

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