Absorbance spectrum of Ninhydrin curve1,61,41,20,80,60,40,2100200300400500600700800900-0,2Wavelength nm- Arginine- Proline-Leucine2. Discuss the absorption spectra of the 3 amino acids as given in graph 1.1.Absorbance (OD)

Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Answered: Absorbance spectrum of Ninhydrin curve…

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

pleassseeee help im confused thank u
how to i draw this following lipid at PH 7.4. N-palmitoyl-D-erythro-sphingosylphosphorylcholine (aka16:0 sphingomyelin). thank you!
How much agarose need for 40 mls of 1.5%w/v gel
Leu 93 Val 49. Are these two residues polar or hydrophobic (nonpolar)? What effect should their proximity have on the pKa Lys 216 Schiff base?
32
42 please dont reject it, u are expert u can answer this
Non-enzymatic browning Proteins: Lysin, methionine Sugars: glucose, galactose, sucrose, fructose, maltose 1. Describe (the aromas produced) and the degree of browning for each solution 2. Explain variations in color with respect to each sugar-amino acid combination by taking the chemical structures of sugars and amino acids into consideration
On Dimyristoyl phosphatidylserine, Palmytoyl-Oleoyl Phosphatidylcholine and Sphingomyelin, What is the capacity of each of these to form hydrogen bonds with its neighbours
Can you draw the following. Around what's it suppose to look like. 1.) Clean Surface: [Gold surface of SPR]• SAM Formation: Gold surface - S - (CH2)11 - OH• Activation: Gold surface - S - (CH2)11 - CHO (using PCC)• Carbohydrate Coupling: Gold surface - S - (CH2)11 - CH=N - Carbohydrate (followed by NaBH3CN reduction) 2.) Clean Surface: [Gold surface of SPR]• SAM Formation: Gold surface - S - (CH2)11 - OH• Activation: Gold surface - S - (CH2)11 - CHO (using PCC)• Carbohydrate Coupling: Gold surface - S - (CH2)11 - CH=N - Carbohydrate (followed by NaBH3CN reduction)
Titration curve of an unknown amino acid The graph below shows a curve, which was obtained following titration of an unknown amino acid. Include a suitable descriptive title stating the identity of the unknown amino acid Use rectangles to precisely outline the regions in the graph where ionisable groups show buffering activity (base/acid ratio 1:10 to base/acid ratio 10:1); clearly associate the name of the ionisable group with the buffering regions; indicate within the graph all observable titration mid-points and all observable titration end-points and indicate estimates of the pKa of the three functional groups (do not provide pka values from the literature, you need to read the pka from the titration curve provided). Note that it is not possible to estimate the pka with more than one decimal precision due to limited resolution of the shown graph.
Structures PLEASE DRAW OUT THE FATTY ACIDS - Hydrocarbon chain atoms DO NOT need to be labeled, everything else does. Common name Symbol Lauric acid 12:0 Myristic acid 14:0 Palmitic acid 16:0 Stearic acid 18:0 Arachidic acid 20:0 Palmitioleic acid 16:1 △9 Oleic acid 18:1 △9 Linoleic acid 18:2 △9,12 a-Linolenic acid 18:3 △9,12,15 g-Linolenic acid 18:3 △6,9,12 Arachidonic acid 20:4 △5,8,11,14
TRUE OR FALSE 1. In the structure of Aztreonam, addition of a moiety capable of Van de Waals interaction confers stability against beta-lactamases 2. Addition of an acyl amino group to carbapenems increases their resistance to acid degradation, thus, making them stable in an oral dosage form 3. In the core structure of monobactams, the methyl group cannot be rotated because of its attachment on the beta lactam ring. The structure is too rigid for the methyl group to be rotated

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

Absorbance spectrum of Ninhydrin curve 1,6 1,4 1,2 0,8 0,6 0,4 0,2 100 200 300 400 500 600 700 800 900 0,2 Wavelength nm Arginine Leucine Proline 2. Discuss the absorption spectra of the 3 amino acids as given in graph 1. Absorbance (OD)