CAS BI 108 Study Guide - Quiz Guide: Covalent Bond, Atp Synthase, Endergonic Reaction

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peanutgirl123

12 May 2023

School

Boston University

Department

Biology

Course

CAS BI 108

Professor

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Document Summary

Posttranslational modification amino acidsjoinedtogetherby ribosome into peptidesin a process called translation aftertranslation amino acids can be covalently f modified example ppgsinceit isaftertranslation modificationsarenotdonebyribosomes. Bonds theyform in proteins to enhancestructuralstability cysteinemolecules in polypeptide chain. H d cha su su che d y. I alleathis blethere"s furs band together c j. Genergy defined as constanttemple constant pressure constant temp 6 constantpressure. Nowdiff teena ah ago when a reaction is at equilibrium when do do negative free energy rtleased in reaction. Favorable aka spontaneous exergonic trolling a ball down a hill. When dg ago positive freeenergy consumed in reaction. Unfavorable aka endergonic nonspont aneous putenergy in products a. Dito enthalpy u heat energy sum of all bondenergies a noncovalent interactions. C heat given off favorable to dao heat given off goingfrom substrates toprodus. H favorable to our more disorder less order favorable. Enzymes are catalysts increase reactionrate bylowering transitionstale energy dat. Agienergydifferencebetweenreactions translationstate the action coordinate diagram: transitionstaleenergy enzymecatalyzed i .

Related Questions

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

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

Proteolytic processing is a(n)

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

1 points

QUESTION 8

In a major protein degradation pathway in the cell, a short polypeptide called ___________ is attached to a protein to target it for destruction

	a.	Ubiquitin
	b.	Ubiquinone
	c.	Disulfide Isomerase
	d.	Signal Peptidase
	e.	Glutathione

olivepig242

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

1. Describe the effects of post-translational modifications to specific amino acids on the 3D structure of a protein. Consider the following modifications: phosphorylation at Ser or Thr residues, glycosylation, acetylation of Lys residues, oxidation of sulfhydryl groups, hydroxylation, and proteolysis. Do you know of any other types of chemical modifications on proteins? If so, what are they and how do they modify proteins?

2. Why does virtually every protein contain âunstructuredâ loops?

ambermule683

CAS BI 108 Study Guide - Quiz Guide: Covalent Bond, Atp Synthase, Endergonic Reaction

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