. A protein gives, under conditions of buffer composition, pH, and tem-perature that are close to physiological conditions, a molecular weightby sedimentation equilibrium measurements of 140,000 g/mol. Whenthe same protein is studied by SDS gel electrophoresis in the absenceor presence of the reducing agent B-mercaptoethanol (BME), the pat-terns seen, respectively, in lanes A and B are observed. Lane C containsstandards of molecular weight indicated. From these data, describe thenative protein, in terms of the kinds of subunits present, the stoi-chiometry of subunits, and the kinds of bonding (covalent, noncova-lent) existing between subunits. /AB- BME+ BMESTDSerum albumin,67,000Ovalbumin,43,000Carbonic anhydrase,30,000Trypsin inhibitor,20,000102.4.Cocm migrated

Given values: The given molecular weight of the native protein (Under physiological conditions) =…

Answered: . A protein gives, under conditions of…

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

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you are ready to elute your MBP-BAP protein from the column using 1.5mL of TBS + 10mM maltose. Create a buffer from the provided 1x TBS and 500mM maltose stock solution.
PLEASE have the following and help D:. What i need for the chosen of 2/3 choices. 2) Illustrate detailed chemical scheme for how you will functionalize your biomolecule to the surface of the sensor (e.g. if you wanted to functionalize a protein to a gold SPR chip, you should could show the assembly of an amine-terminated SAM, followed by carbodiimide coupling of. the protein). These schemes should be drawn using a chemical illustration software package (ChemDraw / ChemSketch).Your chemical schemes should be as detailed as necessary to accurately depict the chemical design of your system, DO NOT INCLUDE a step-wise mechanism, it is not necessary. You should include at least one literature reference to support your conjugation strategy.3) Include an illustration of the functional sensor, and describe whether the sensor is label-free or not, what signal is observed, and how you would detect the interaction (i.e. if a labeled antibody is required, you should describe what label would…
i. What are the advantages of biological value of protein method compared to N-balance and chemical score? ii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N in the faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacal nitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively. Calculate the BV of the protein in the diet.
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.
Suppose you have a concentration of 356ng/uL for Sample A. How many ng of protein will that be?
In quantitative determination of protein using spectrophotometer how can I plot the absorbance vs wavelength for the proteins given the transmittance values?

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