Proflavine was used to treat wounded soldiers in the Far East during the second world war. Which of the following statements is false regarding proflavine!H₂N7NH₂Its target is located in the cell membrane.Its planar shape is important to intercalation.The primary amine groups are protonated and interact with phosphate groups of the DNA backbone.When inserted into DNA, the tricyclic system can form van der Waals interactions with base pairs above and below it.

A derivative of acriflavine, proflavine is bacteriostatic and disinfecting against a wide variety of…

Answered: Proflavine was used to treat wounded…

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

See similar textbooks

Similar questions

Please answer the following questions 1) based on the structures of adenine, cytosine, guanine, and thyme. Why does A prefer to bind to T and C prefer to bind to G 2) were the binding energies the same for AT and CG? Explain the difference 3) which of the four know bases is the unknown synthetic base most like in terms of its binding characteristics? What does this indicate about its structure? 4) if the unknown synthetic base was used to study DNA replication, which natural bases would it interact with? 5) is the picture question
The enzyme cytidine deaminase catalyzes the conversion of cytidine to uridine. Cytidine deaminase catalyzes the reaction through an addition of water across the cytidine 3,4-bond, forming a tetrahedral intermediate followed by the elimination of NH3 to form the product uridine. This is like the addition-elimination mechanism that we studied for adenosine deaminase. Cytidine deaminase НО. NH₂ N пOH OH cytosine R + H₂O cytidine The Km value for the substrate cytidine is 2.5 × 10-4 M, and the K; for competitive inhibition by the product uridine is 2.5 × 10-³ M. N R A reduced derivative of the product, 3,4,5,6-tetrahydrouridine was shown to be a fully reversible competitive inhibitor with a Ki of 2.4 x 10-7 M, a value approximately 10,000 times lower than that of the product uridine. NH₂ NH uridine HO. N R R = D-ribose HOH OH uridine 3NH uracil ring numbering H NH H H + NH3 H OH H 3,4,5,6-tetra- hydrouridine a.) Draw a structure of the intermediate that we predict to form during the…
A toxin is glycopeptide, X that is composed of an octapeptide and a saccharide Y. Glycopeptide X is composed of a glycan Y and an octapeptide. The octapeptide was cleaved by trypsin, giving 2 tetrapeptides of exactly the same composition except for its N-terminals. When the octapeptide was cleaved by chymotrypsin, it gave a pentapeptide and a tripeptide. DNFB treatment gave DNP-ser. The composition of the octapeptide is lys, ser, trp.and leu. The leu:ser ratio is 4:1. 1. What is the sequence of this octapeptide? Saccharide Y is a tetrasaccharide. To determine its linkages, a person methylated glycopeptide X effectively methylating saccharide Y. Cleavage gave the peptide and the following products: 2,3,4-tri-O-methyl-a-D-glucopyranoside acid, 2,3-di-O-methyl-ß-D- glucopyranoside, 1,3,4-tri-O- methyl-ß-D-glucuronic acid treatments to the isolated tetrasaccharide gave the following results: and 1,4,6-tri-O-methyl-ß-D-N- acetylgalactosamine. Further 1. A. Treatment of saccharide Y with an…
In a gel electropherosis, Glutamate and valine created a double bond. How is that possible?
A decapeptide which could resist burns was isolated from an endemic plant from Mt. Mayon. Deduce the amino acid sequence of the decapeptide given the following informations. Mercaptoethanol gave two pentapeptides F1 and F2. Chymotrypsin treatment of F1 releases S and a tetrapeptide (C,K,F,M) while F2 gave a dipeptide (M,S) and a tripeptide (C,F,K) F1 when treated with CNBr released a free homoserine lactone and a tetrapeptide. Trypsin treatment of F1 gave a tripeptide and a dipeptide. F2 treated with carboxypeptidase released free M while with trypsin gave free K and a tetrapeptide.
Given the following diagram of how protein AWESOME1 binds to it's target DNA, describe the potential effects of each of the 5 mutations shown below. The wild-type sequence of a helix #1 is also shown in the blue box, and all the mutations are in helix #1 (see numbers for identifying particular residues). a helix #1 R(1)-V-I-L-Y-F-W-I-M-Y-F-S-H-Y-W-R(16) #1 Predict the consequence of the following mutations: 1) Arg(1) to Glu 2) Arg(1) to Ala 3) Phe(6) to lle 4) Trp(7) to Phe 5) Met(9) to Pro in
What is the role of his119 in the RNase-catalyzed hydrolysis of RNA, as indicated in the Figure below? RNA -0-CH₂ Q Base His 119 H H NH His 12 -P-0-CH₂ a Base H H 3' H O 2' O-H OH O -0-P=0 It acts as a general base, abstracting a proton from the 2' hydroxyl in order to increase its nucleophilicity. It forms an H-bond with his12 in order to stabilize the transition state. It serves as a general acid, donating a proton to improve the quality of the leaving group. It works through concerted general acid-base catalysis with his 12 in order to favour the products of the reaction. Two of the above are true.
A tripeptide on selective hydrolysis gives two fragments X and Y. The Fragment X consists of glycine and alanine and fragment Y consists of Valine and glycine. The N-terminal of X is alanine and that of Y is glycine. Identify the tripeptide.
The enzyme creatine kinase catalyzes the ATP-dependent phosphorylation of creatine. Propose a mechanism for the reaction described using the curved arrow convention. Show the complete structure of the nucleotide.
Posttranslational modifications of proteins do not include: peptide bond formation glycosylation acetylation of N-terminal peptide bond cleavage disulfide bond formation QUESTION 16 14 15 16 streptomycin puromycin 17 18 19 20 Which one of the following antibiotics does NOT function by interfering with the translational/post-translation process tunicamycin penicillin O tetracyclin O O
Using abbreviations (not structures), write the reaction of flavin adenine dinucleotide that gives off energy (-AG). Match the items in the left column to the appropriate blanks in the equation on the right. H+ FADH → FADH3 + H+ 3/2H2 FADH3 FAD FADH 2H+ FADH2 3H+ H2
Which of the following statements comparing the synthesis of pyrimidines vs. purines is correct? (A) Both types of nucleotides are formed by constructing the nitrogenous base step-by-step on a phosphorylated ribose foundation.(B) Aspartate serves as a nitrogen donor only for purines, while pyrimidines use only glutamine as a nitrogen donor. (C) Both pathways require the synthesis of 5-phophoribosyl-1-pyrophosphate.(D) During the de novo synthesis of both types of nucleotides, nucleosides are formed first and then phosphates are added to the 5’ carbon of ribose.(E) Ribonucleotide reductase is used to form dNTPs from pyrimidine NTPs but not purines.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS