Lehninger Principles of Biochemistry 7E & SaplingPlus for Lehninger Principles of Biochemistry 7E (Six-Month Access)
Lehninger Principles of Biochemistry 7E & SaplingPlus for Lehninger Principles of Biochemistry 7E (Six-Month Access)
7th Edition
ISBN: 9781319125882
Author: David L. Nelson, Michael M. Cox
Publisher: W. H. Freeman
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Chapter 4, Problem 8P
Summary Introduction

To determine: The number of amino acids which is required for one segment of α-helix to transverse membrane completely and estimate the fraction of bacteriorhodopsin protein which is involved in membrane-spanning helices.

Introduction:

Amino acids are important biological molecules that are involved in the regulation of several cellular processes of body. It is an organic compound that contains an amine group and carboxyl group along with a function R group.

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The beta-lactamase hydrolyzes the lactam-ring in penicillin. Describe the mechanism  of hydrolysis, insuring to include the involvement of S, D, & K in the reaction sequence. Please help
To map the active site of beta-lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine. Why doesn't D in this hexapeptide not participate in the hydrolysis of the beta-lactam ring even though S, K, and D are involved in the catalyst?
To map the active site of -lactamase, the enzyme was hydrolyzed with trypsin to yield a hexapeptide (P1) with the following amino acids. Glu, Lys, Leu, Phe, Met, and Ser. Treatment of P1 with phenyl isothiocyanate yielded a PTH derivative of phenylalanine and a peptide (P2). Treatment of P1 with cyanogenbromide gave an acidic tetrapeptide (P3) and a dipeptide (P4).Treatment of P2 with 1-fluoro-2,4-dinitrobenzene, followed by complete hydrolysis, yields N-2,4-dinitrophenyl-Glu. P1, P2, and P3 contain the active site serine.  Using the experimental results described above derive the primary sequence of the active site hexapeptide. Please help!
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The Cell Membrane; Author: The Organic Chemistry Tutor;https://www.youtube.com/watch?v=AsffT7XIXbA;License: Standard youtube license