In this diagram of the first step in the reaction catalyzed by the protease chymotrypsin, the process of general base catalysis is lustrated by the number and the process of covalent catalysis is Illustrated by the number Chymotrypoin s میرا R-N 1; 2 2; 3 2:3 3; 2 (D) 1;3 HO ||| HO Ser DH Ser WH

In this diagram of the first step in the reaction catalyzed by the protease chymotrypsin, the process of general base catalysis is lustrated by the number and the process of covalent catalysis is Illustrated by the number Chymotrypoin s میرا R-N 1; 2 2; 3 2:3 3; 2 (D) 1;3 HO ||| HO Ser DH Ser WH

Chemistry: Principles and Reactions

8th Edition

ISBN:9781305079373

Author:William L. Masterton, Cecile N. Hurley

Publisher:William L. Masterton, Cecile N. Hurley

Chapter23: Organic Polymers, Natural And Synthetic

Section: Chapter Questions

Problem 44QAP: A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of...

See similar textbooks

Similar questions

A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)
provide brief explanation thnks
The shaded area in the following diagram shows CH₂ CH | H CO-H-N N-H-O -CH₂ C-OH-N Gly 193 H RN Covalent bond formation between a catalytic amino acid residue and the substrate during chymotrypsin catalysis. Acid-base catalysis by a catalytic residue in chymotrypsin. Oxyanion hole which stabilizes substrate binding in chymotrypsin catalysis. Oxyanion hole which stabilizes transition state in chymotrypsin catalysis. Low barrier hydrogen bond formation between the transition state and one of the catalytic residues of chymotrypsin. ?
The activity of an enzyme requires a glutamic acid to display its -COOH functional group in the protonated state. Suppose the pK, of the -COOH group is 4.07. (a) Will the enzyme be more active at pH 3.5 or 4.5? Explain. (b) What fraction of the enzymes will be active at pH = 4.07? Explain. (c) At what pH will the enzyme show 78% of maximal activity?
If a solution of compound X is ncubated with a catalytic anount of enzyme Y the sucrose is trarsformed to glucose aid Euctose in the reaction 1X 1 fedose3 ghacose A eqahum, The concenttons of the seation comgoests he and 2mM glucose. What is Keg? Oa, 6 Ob4 Oa 20 O'd. 5 A Moving to another question wili save this response.
What is the ratio of CATION to ANION in Drug X? [blank1] H₂C -H Fogy CH3 SO42 'N CH3 Drug X CH3NH Describe the possible interactions between the SIDE CHAINS of amino acids: I. and II.... II. and III... I. and III... 1. COO NH3* 2 HO II. COO HO NH3* COO NH3* III.
In carbonic anhydrase II, Zn* acts as a Lewis acid coordinated in the enzyme active site to histidines in a tetrahedral geometry for peptide bond cleavage. * True False
(Thanks for the help if you can break down the steps and provide drawings(needed) during the answer since i am trying to see if i have solved this in the right way not copy :)) Draw the heme environment in oxymyoglobin and explain how the geometric data for the attached oxygen molecule may be understood. Fe O (bond length) = 1.809 Å; O-O (bond length ) = 1.246 Å; Fe - O - O (bond angle) = 123 \deg
Q: 1.5%. Sucrose by massx M what volume f soft,dmink Solin Noitolu millimeter contain' 5:29 of Suvrose bolovitine 102 102 24A) nioino) 220 ud s d ro tnaroa 220M 220m V
An enzyme catalyzes the hydrolysis of an ester with a certain activity, but this activity is lost in a 3 M urea solution. What is the most likely explanation for the loss of activity? (A) Urea binds to the active site of the enzyme competitively with the substrate. (B) Urea causes the cleavage of the peptide bonds in the enzyme. (C) Urea causes the enzyme to denature and lose its specific three-dimensional shape. (D) Urea reacts with disulfide bonds in the enzyme.
Which of the structures below corresponds to the dipeptide cysteylananine? The parentamino acids are shown below. но H,C-c-8-o NH, но HS-CH, c-¿-o NH, alani ne cysteine но но но "H;N-c-C-N-c-&- ČH; H CH; A. B. CH, H CH, SH SH H,C O но нс о "H,N-c-E-N-c-&-o H CH; но C. "H,N-c-c-N-ċ-E-o SH SH O H "H,N--ċ-o-o-ċ- E. c-NH" 'H. ČH, SH D.
10) Can H3PO4 exist with H₂PO4 in a mixture? What about H₂PO4 and HPO4²? What about H₂PO4 and PO,³?