Q7. Propose a structure that is consistent with each set of data.a. C4H100 1H NMR spectrum singlet & 1.28 (9H) singlet & 1.35 (1H)b. C7H15CI 1H NMR spectrum singlet 8 1.10 (9H) singlet 8 1.60 (6H)c. C2H4Br2 1H NMR spectrum doublet & 2.50 (3H) quartet 8 5.90 (1H)d. C4H8C12 1H NMR spectrum doublet 8 1.60 (3H) quartet 8 2.15 (2H) triplet 8 3.72 (2H) sextet 84.27(1H)

Approach to solving the question:a. C4H10O 1H NMR spectrum:Singlet at δ 1.28 (9H): This suggests a…

Answered: Q7. Propose a structure that is…

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

3. A. Give steps with equations of Chain (or radical) polymerization reaction for fabrication of polyethyl acrylate. B. Discuss how do free radicals effect living organisms and cells.
OO HUAWEI nova 2 Plus DUAL CAMERA Specificity is one important characteristic of any Molecular Detection System and means: Select one: O a. The test must be able to detect large amounts of target O b. The test yields a negative result for the target molecule only O C. The test must be able to run efficiently and inexpensively on a routine basis O d. The test must be able to detect small amounts of target e. The test yields a positive result for the target molecule only In the somatic cells of the body which of the following can have an impact on gene expression to protein? a. miRNA genes Ob. RNAI C. d. gene knockout by CRISPR e.
. Brifely describe the difference between Zero oreer, First order and Hugher order NMR Spectra??
Remember that DNA is a sequence of the letters A,C,T, and G. A binds with T and C binds with G. Solutions are specified by the DNA sequence, such as ACAC or TG, and by the concentration in units of micromolar (uM = 10-M) Consider mixing 30ml of 0.30µM ACAC with 45ml of 0.50pM TG. Predict what reactants and products should be present in the final solution and then check your answer in the virtual lab. (Please give your final answer in total nanomoles (10 moles) for each species in the solution)
Match the following protein descriptions with the method that is best for determining the structure. A 20 amino acid peptide hormone An entire viral particle A 30 kDal nuclear hormone receptor A 18 kDal protein that assembles into a 24-mer structure with a molecular weight of 600 kDal A 15 kDal protein that appears to be extremely flexible A. NMR B. X-Ray Crystallography C. Cryo-EM
which in is the best method for separating proteins A and B that have the properties below: Protein A: a tetramer of identical 80kDa subunits with a pl of 6.4 Protein B: a monomeric protein with a MW of 80kDa and a pl of 9.2 A.) Anion exchange chromatography at pH 11 B.) Gel exclusion chromatography C.) Cation exchange chromatography at pH 4 D. Cation exchange chromatography at pH 11 E.) SDS-PAGE
. Suppose you have two genetic variants of a large protein that differ only in that one contains a histidine (side chain pk, = 6.0) when the other has a valine (uncharged side chain). (a) Which would be better for separation: gel electrophoresis or isoelectric focusing? Why? (b) What pH would you choose for the separation?
(a) 1 Normalized fluorescence 0.8 0.6 0.4 0.2 0 50 55 OM 0.100 M 0.200 M 0.300 M 0.500 M 1.00 M 2.00 M 60 113588 65 Temp. (°C) 70 75 80 Where is fully folded protein? • Where is fully unfolded protein? • Where is partially folded protein? • To what does SYPRO orange bind? • Why does fluorescence increase as a function of temperature? ● Define a melting temperature for a protein. • Demonstrate how an estimated melting temperature of the protein in zero molar ligand can be determined. • What is the effect of increasing the molar concentration on melting temperature for this protein? • Why is melting temperature a useful measurement to make for a protein especially if you are interested in protein aggregation?
. Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and IIVD. None is true
The extinction coefficient or absorptivity (ɛ) of protein A at 340 nm is 6440 M-1 cm-1, whereas protein B does not absorb at 340 nm. What absorbance will be observed when light at 340 nm passes through a 5 mm cuvette containing 10 µM of protein A and 10 µM of protein B? Beer-Lambert-law; A = ɛ x C x1; A = absorbance, C= concentration, 1= pathlength).
Define the following terms: a. phosphoryl group transfer potential b. adenosine c. adenosine monophosphate d. high-energy bond e. resonance hybrid
3. In what direction (toward the anode, toward the cathode, or toward neither) will the following proteins move in an electric field? a. Serum albumin (pl=4.9) at pH 8.0 b. Urease (pl=5.0) at pH3.0 and pH 9.0 c. Ribonuclease (pI=9.5) at pH 4.5, 9.5 and 11.0 d. Pepsin (pl=1.0) at pH 3.5, pH7.0 and pH 9.5

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