**Question 31***True/False Question:*Side chain of a serine residue in the active site of an enzyme can serve as a nucleophile during the catalysis.- ○ True- ○ False

The amino acids present in the active site play a vital role in the mode of enzyme catalysis. The…

Answered: True/False Question: Side chain of a…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Can you please solve the following question, both parts please.
200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.
Define the word "enzyme inhibition."
How temperature, pH and salt affects the enzyme activity in terms of protein structure (primary, secondary, tertiary, quaternary) and other factors? Please explain briefly.
How can we tell if the enzyme has been denatured by a particular temperature treatment.
Consider the reaction coordinate diagram shown below. X is is Catalysts lower the amount of energy required to reach the transition state (the activation energy) Energy Ground state of reactant Reaction coordinate AG of catalyzed reaction AG of the reaction Ground state of product ; Y
Please handraw this graph with all the necessary detailed information: Imagine that I text enzyme rate for four different temperatures: 10 degrees celsius, 20 degrees celsisus, 30 degree celsius, and 40 degree celsius, in separate tubes. The enzyme appears to work faster as temperature increases, but completely ceases activity at 40 degrees celcius. Sketch a graph to show this outcome, but here you will graph product formation (nmoles/mL) vs. time (minutes). The graph should be 4 lines and HANDDRAWN. Include a legend if necessary. You do not need precise quantitivate values, but most show the correct trends on the graph.
Which of the following describe what enzymes such as Chymotrysin accomplish to allow products to form and be released by the enzyme active site? Group of answer choices catalyze chemical eactions that are thermodynamically unfavorable to occur establish a more stable transition state at a higher energy level to perform a catalysis reaction redce the chemical energy held within a chemical bond modify chemical structure of a substrate to "fit" within the active site
An E. coli cell with a non-functional FtsH protease would be expected to: Be unable to initiate a heat-shock response O Be unable to turn off the heat shock response once started Be able to mount a fully functional heat shock response Be unable to fix misfolded proteins during the heat shock response
Catalysis through proximity and orientation effects involves: (select all that applies) Group of answer choices binding of acidic and/or basic groups in the binding site facilitating chemical reactions by binding substrates close to specific groups binding of substrate in specific, restrictive orientations depending on metal ions for catalysis
Kindly refer to the photo attached. thank you
None

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True/False Question: Side chain of a serine residue in the active site of an enzyme can serve as a nucleophile during the catalysis. O True O False