Help? Which statement below about Bradfordassay is wrong?O Coomassie Brilliant Blue dye is used tobind certain proteins specifically.BSA is used to make standard curve.Unknown protein concentration can becalculated once BSA standard curve isgenerated.O Similar to A280, Bradford assay is used todetermine total protein concentration. Which statements about common buffersystems use in biochemistry labs isincorrect?O In the pKa region of a buffer solution, pHchanges greatly as H+ or OH- is added.O Buffer systems resist large pH changes.O Common buffer systems contain conjugateacid and base.O pH of any buffer solutions does change.

You have asked 2 questions. I will answer 1st question, as per guidelines. The Bradford assay is…

Answered: Which statement below about Bradford…

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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How would you determine the concentration of a protein that falls outside (above or below) the linear range of this assay? asap
V-max is correctly defined as: a) Km b) The fastest velocity achieved during an enzyme assay, usually at the beginning of the assay. c) V-init when [S] = Km. d) The fastest velocity achieved during an enzyme assay. This can be at any point during the assay. e) V-init at very high concentration of substrate.
What are the advantages of the yeast-two-hybrid system over other in vitro methods used for protein-protein interactions? (select all that applies) enhanced sensitivity heavy dependence on antibody use no bias towards high affinity interactions precipitation of proteins of interest
Match the types of data to the example. Precise measurements Assay standard Positive control Quantitative results Negative control Qualitative results Standard curve…
A protein gives a single band on SDS gel electrophoresis, as shown in lanes 1 and 2 below. There is little, if any, effect from adding β-mercaptoethanol(BME) to the sample; if anything, the protein runs a little bit slower. When treated with the proteolytic enzyme thrombin and electrophoresis in the absence of BME, the protein migrates a bit more rapidly (lane 3). But if BME is present, two much more rapidly migrating bands are found (lane 4). Explain these results in terms of a model for the protein.
The following assays is/are considered a DIRECT ASSAY: A. absorbance B. рн C. Viscosity D. All of the above Which of the following is/ are statement/s NOT describing enzyme activity? A. Activity is inversely proportional to the concentration B. It is a reflection of its concentration C. It is commonly measured in terms of their catalytic activity D. None of the above What is the difference between enzymes from antibodies? A. ability to bind with compounds with great specificity and high affinity B. bind in high energy state C. binds the complementary structure in its ground state D. All of the above
why are lysozyme and ovoalbumin the recommended standards used in the Bradford protein assay and why would they be preferred over BSA being this widely used but not recommended? Justify the answer
Experiment: Bradford protein assaygive the answers (4-5 lines) of review questions in the end. answer should be logical and understandable and without plagiarism. avoid copy pasting. Background information:The Bradford assay is very fast and uses about the same amount of protein as the Lowry assay. It is fairly accurate and samples that are out of range can be retested within minutes. The Bradford is recommended for general use, especially for determining protein content of cell fractions and assessing protein concentrations for gel electrophoresis. The method described below is for a 100 µl sample volume using 5 ml color reagent. It is sensitive to about 5 to 200 micrograms protein, depending on the dye quality. In assays using 5 ml color reagent prepared in lab, the sensitive range is closer to 5 to 100 µg protein. Scale down the volume for the "micro assay procedure," which uses 1 ml cuvettes. Protocols, including use of microliter plates are described in the flyer that comes with…
You overexpressed (asked bacteria to make a lot of) an 80 kDa protein carrying a 6X-His tag and purified it on a nickel column. You collect frac ons from your purifica on and analyze them using SDSPAGE. The results are shown in image attached. a) Interpret the results from the gel. What is wrong? (see image attached) b) Identify 2 possible reasons why this problem is occurring, and for each reason, suggest an experimental modifica on you can do to troubleshoot.
Identify two other methods of protein content determination and differentiate them from the Bradford assay
is bradford assay using dye Coomassie Brilliant Blue G-250 a different method from using a spectrophotometer ? if so how is it different to determine protein concentration?
That is the lactase assay Calculate initial rate

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