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Chapter 8, Problem 2P
Summary Introduction

To determine: The base sequence of the given complementary strand.

Introduction:

There are two types of nitrogenous bases: purines and pyrimidines. Adenine and guanine are the purine bases with double ring structures. Cytosine and thymine are the pyrimidines bases that have single ring structure. These bases pair with their complementary bases and form a nucleotide sequence through hydrogen bonding.

Summary Introduction

To determine: The special type of sequence which is contained in the DNA segment.

Introduction:

Some DNA segments have regions with inverted repeats which are in such way that an inverted and sequences which are self-complementary in a strand is repeated in the opposite direction in the complementary strand. This DNA segment is known as palindrome.

Summary Introduction

To determine: Whether the double-stranded DNA has the potential to form any alternative structures.

Introduction:

Some DNA sequences adopt unusual structures. The sequence dependent structural differences which are found in large chromosomes could affect the metabolism and function of nearby DNA segments.

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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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