BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG
BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG
1st Edition
ISBN: 9780134172507
Author: APPLING
Publisher: Pearson Education
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Chapter 9, Problem 8P
Interpretation Introduction

Interpretation:

The structure of GlcUAβ(13)GlcNAc units are connected with β(14) should be determined.

Concept introduction:

A Haworth projection is common way to represent the cyclic structure of monosaccharides.

Five and six member hemiacetals are represented as planar pentagons or hexagons.

α form of the Haworth projection indicates, the exocyclic O group at the anomeric center is on the opposite face as to the CH2OH group.

β form of the Haworth projection, the exocyclic O group at the anomeric center is on the same face as to the CH2OH group.

In the Haworth projection - CH2OH group is present in the RIGHT side of the ring is called D- form.

In the Haworth projection - CH2OH group is present in the LEFT side of the ring is called L- form.

For example:

Haworth projections of glucose:

BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG, Chapter 9, Problem 8P , additional homework tip  1

Pictorial representation:

The structure of Hyaluronic acid where GlcUAβ(13)GlcNAc units are connected with β(14) is as follows.

BIOCHEMISTRY BOOKS ALC&MOD MST/ET PKG, Chapter 9, Problem 8P , additional homework tip  2

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Students have asked these similar questions
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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