+ BC367, Fall 2009 Exam 2 Review Questions. + In Anfinsen’s experiment, RNAse was denatured with urea and β -mercaptoethanol. After dialysis and treatment.

Slides:



Advertisements
Similar presentations
Enzyme Activity The properties of enzymes related to their tertiary structure.The effects of change in temperature,pH,substrate concentration,and competitive.
Advertisements

E N Z Y M E S What are they? What do they do? How do they work?
ENZYMES: KINETICS, INHIBITION, REGULATION
Protein Function Structure will determine the function of the protein.
Protein Structure/Function C483 Spring Proteins segments which fold first can promote the folding of other sections of the protein into the native.
Biochemistry Enzymes.
Mr. Safford’s Biological Sciences.  All enzymes are globular proteins thus spherical in shape  Control biochemical reactions in cells  They have the.
 The active site have a rigid shape.  Only substrates with the matching shape can fit.  The substrate is a key that fits the lock of the active site.
Ahlfors and Mansour studied the activity of purified sheep phosphofructokinase (PFK) as a function of the concentration of ATP, in experiments that were.
Free Response Questions
Enzymes What is it?? Enzymes are PROTEIN molecules. Protein molecules are composed of one or more amino acid chains, folded into uniquely shaped globs.
Two Substrate Reactions
16.6 Factors Affecting Enzyme Activity
Enzymes.
Web Quest.  Enzymes are proteins that speed up chemical reactions in the body.
{ Enzyme Inhibition Why enzymes don’t work.  An enzyme is just a folded protein Remember!!!
ENZYME KINETIC M. Saifur R, PhD. Course content  Enzymatic reaction  Rate of Enzyme-Catalyzed Reactions  Quatification of Substrate Concentration and.
Enzymes Mrs: Jackie. Enzymes A biological catalyst that speeds up chemical reactions in the body by lowering the energy needed in the reaction Globular.
Background on Chemical Reactions Section 2.4 of the Textbook.
ATP Immediate source of energy that drives cellular work Adenosine triphosphate Nucleotide with unstable phosphate bonds Phosphate bonds easily hydrolyzed.
Catalysts of Life. Review of Chemical Reactions A chemical reaction is a process that changes, or transforms, one set of chemicals into another Reactants.
LEHNINGER PRINCIPLES OF BIOCHEMISTRY
Lecture 4 Web: pollev.com/ucibio Text: To: Type in:
Review session for exam-III Lectures The concept of “induced fit” refers to the fact that: A. Enzyme specificity is induced by enzyme-substrate.
ENZYMES. are biological catalyst are mostly proteinaceous in nature, but RNA was an early biocatalyst are powerful and highly specific catalysts.
Why are enzymes important to living things?
PROTEINS (Polymers of Amino Acids)
ENZYMES. Enzymes are proteins that act on a substance called a substrate. enzyme substrate > product In the above reaction the enzyme's active.
Active Sites – What’s Happening? 1. Substrate is bound 2. A reaction is being catalyzed.... e. g.
Enzymes are protein molecules that are able to catalyse a biological reaction.
6-1 Unit E: Enzymes. 6-2 An enzyme is a protein molecule that functions as an organic catalyst to speed a chemical reaction. An enzyme brings together.
Lecture 4 Enzymes. Proteins Catalyze all cellular reactions Enzymes are not changed by the reactions, and can be reused.
ENZYMES. < < < < < < Controlling Enzyme Activity Competitive Inhibition A substrate mimic (molecule that has the same configuration as the.
AH Biology: Unit 1 Proteomics and Protein Structure 3
Enzymes A protein catalyst Enzymes are important proteins found in living things. An enzyme is a protein that changes the rate of a chemical reaction.
Lock and Key Model Enzymes are specific to their substrates Substrate and active site match each other in two ways: Structurally  substrates that don’t.
Themes: Structure meets Function
Protein Structure Primary - sequence of amino acids Secondary – folding into pleated sheets or alpha helix Tertiary – 3-D structure, completely folded.
Draw sketch graphs for enzyme activity with a competitive inhibitor present and for a non-competitive inhibitor present.
Chemistry: An Introduction to General, Organic, and Biological Chemistry, Eleventh Edition Copyright © 2012 by Pearson Education, Inc. Chapter 16 Amino.
Mammalian Transport System
Investigation of the enzymatic processes depending on the type of reaction.
Proteins.
Factors that Affect the Rates of Enzyme catalyzed Reactions [Enzyme] - ↑ [E], ↑ rate [Enzyme] - ↑ [E], ↑ rate [Substrate]- ↑ [S], ↑ rate only up to a point.
Enzymes Definition and Classification
Enzymes.
ENZYMES: KINETICS, INHIBITION, REGULATION
BIOLOGY PROTEINS.
Enzymes.
Enzymes Regulatory enzymes are usually the enzymes that are the rate-limiting, or committed step, in a pathway, meaning that after this step a particular.
Enzymes.
Biochem (Test 1) 11. Which of the following statements most directly supports the claim that different species of organisms use different metabolic strategies.
Enzymes Learning Outcome B11.
Enzymes Key to Metabolism.
Chemical Reactions Review
Enzymes.
Metabolic reactions are regulated in response to the cell’s needs.
Enzymes.
Metabolism 8.1.
Enzymes.
Enzymes Homeostasis: property of living organisms to regulate their internal environment, maintaining stable, constant condition *Occurs by multiple adjustments.
What are the factors affecting Enzyme Activity?
Enzymes.
2.5 - Enzymes.
What DNA sequence codes for this chain of amino acids...?
Enzymes.
Enzyme Kinetics Velocity (V) = k [S]
Enzymes.
Presentation transcript:

+ BC367, Fall 2009 Exam 2 Review Questions

+ In Anfinsen’s experiment, RNAse was denatured with urea and β -mercaptoethanol. After dialysis and treatment with oxygen, the enzyme’s activity was restored. What conclusions can be made from this? a) Urea and β -mercaptoethanol are ineffective denaturants. b) All the necessary information for protein folding is in the primary structure of RNAse. c) RNAse is particularly resistant to denaturation. d) The odds of the enzyme spontaneously folding correctly, with appropriate disulfide linkages, are close to 1. e) There must have been molecular chaperones present to facilitate proper folding.

+ Emperor penguins can remain submerged for up to 18 minutes, diving to a depth of 535 m. What does the oxygen-hemoglobin dissociation curve look like for an emperor penguin compared to the domestic duck? a. The same. The birds have no difference in O 2 binding affinity. b. The dissociation curve is shifted left because the emperor penguin has a higher O 2 binding affinity. c. The dissociation curve is shifted right because the emperor penguin has a lower O 2 binding affinity. d. The dissociation curve is shifted left because the emperor penguin has a lower O 2 binding affinity. e. There is no dissociation curve because birds do not have hemoglobin.

+ You have been invited to join a prestigious relay team competing in a high-altitude 4 x 5k relay. Which of the following would be most helpful so you won’t disappoint your teammates and they’ll want to invite you back again next year? a.Traveling everyday to train at the course up in the Rockies so you can acclimate to the terrain and altitude b.A mutation of His146  Val in the β chain c.Sleeping in a hyperbaric chamber so your body gets used to different pressures d.Renting a house in Denver, but traveling to do most your serious workouts in New Orleans e.Hyperventilating right before the race to decrease your blood pH and help prevent cramps

+ Which is the most likely phenotypic result of Hb mutation Arg141 α -> Cys (Hb Nunobiki)? a) Cyanotic b) Flushed c) Pale d) Normal e) Death

+ Assuming equal enzyme concentrations and based upon the kinetics plot for the substrate S, which of the following enzymes (A, B, C, or D) would have the highest kcat/Km value? A.) A B.) B C.) C D.) D E.) Not enough information to predict

 -Lactamase is an enzyme that conveys resistance to  -lactam antibiotics such as penicillins. For penicillin G, the K M for  -lactamase is 13 μ M. Which of the following plots represents inhibition of the reaction of  -lactamase with penicillin G by clavulcanic acid, a competitive inhibitor? (Concentration units are μ M in all cases.) A. C. D. B. E. 1/v = 1300(1/[S]) /v = 1000(1/[S]) + 130

+ Which of the following is false about the amino acids involved in the active site of chymotrypsin? a) Ser195 acts as a nucleophile. b) His57 acts as a general acid. c) His57 acts as a general base. d) Asp102 influences the pKa of His57 in the presence of substrate. e) None of the above is false.

+ Which of the following is false about enzymes that are made from zymogens? A. Proteolysis results in an active form of the protein. B. Digestive enzymes and blood clotting enzymes are examples of such proteins. C. The protein is inactivated by returning to the proprotein conformation. D. The proprotein may have properties that differ greatly from the final protein. E. Some undergo more than one cleavage event to produce multiple active forms.