In order to study protein structures andfunctions, many protein techniques havebeen developed for specific applications.Which of the following pair of technique:application is INCORRECT?O a.O b.O C.O d.ELISA: protein molecular weightSDS-PAGE: protein molecular weightNMR: protein structurePeptide mass fingerprinting: protein presence andidentificatione. X-ray crystallography: protein structure

There are several techniques that are used to study proteins and understand their structure,…

Answered: In order to study protein structures…

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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Choose the FALSE statement about protein electrophoresis. The proteins in the gel can be visualized by staining them with silver. The distance and speed that a protein moves depend on its shape. Small proteins move rapidly through the gel. It is performed in a thin, horizontal slab of polyacrylamide. The gel serves as a molecular sieve that enhances separation.
A C2 G This a photograph of an actual polyacrylamide gel that has been run with samples of protein. For each question, write the letter from the item in the gel that best matches the word or concept that is described. Answers may be used once, more than once, or not at all. There may be more than one correct answer per question. 1. Band 2. Lane 3. Well 4. Will protein migrate through the gel from A to B or will it migrate from B to A? 5. Which end is nearest the negative electrode, A or B? 6. Which contains smaller protein fragments, F or G? 7. Which letter indicates the highest concentration of protein fragments that are the same size 8. Where would a sample of protein be loaded? B.
Which of the following statements about electron microscopy are true?Group of answer options a.By taking pictures of the same protein frozen in ice thousands of times and then adding them together, you get a high-resolution image of the protein b.Electron microscopy is not used in structural biology as it can not give as high a resolution as X-ray crystallography and NMR c.The smaller a protein, the easier it is to solve its structure with electron microscopy dMost existing protein structures have been resolved using electron microscopy e.The first protein structure with true atomic resolution was solved using electron microscopy last year
The results of a separation using two-dimension gel electrophoresis are shown here. Which protein or proteins have the highest pl value? d and e b and c a Which protein has the highest molecular weight? b d a isoelectric focusing electrophoresis pH 5 a b pH 9 d e SDS PAGE electrophoresis
Mass spectrometry and X-ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to mass spectrometry, X-ray diffraction, or both techniques. Mass spectrometry protein must be conformationally stable X-ray diffraction small amounts of protein are sufficient analysis requires information about the protein-coding gene or genes Answer Bank protein may be denatured requires a large amount of protein protein sample must be pure can detect a covalent modification to a protein Both techniques
Sketch the appearance after visualization of a protein mixture containing the seven proteins above when subjected to two-dimensional (2D) gel electrophoresis.
Compare and contrast the following protein characterization techniques in terms of the principles governing their functions. size exclusion chromatography vs ion-exchange chromatography
a 2D gel electrophoresis was done on the proteins found in the chart. create a chart with the correct parameters on both dimensions using 1-6 to indicate the position of each protein on teh 2D gel.
Suppose you have a cell-lysis sample containing genomic DNA, a complex mixture of proteins, and debris. Describe different commonly used analytical methods to i) analyze the molecular masses of the protein mixture. ii) detect the composition (what specific amino acids are there in what proportion) of a specific protein from the mixture. iii) deduce the sequence of some particular proteins from the mixture content
Which of the following statements are correct about the process of protein structure determination by Cryoelectron Microscopy (Cryo-EM) (select all that apply)? A. Determining a structure by Cryo-EM requires imaging 100s to 1000s of individual protein molecules and using computers to reconstruct 3D images from individual particles B. Requires that proteins form crystals C. Requires freezing of samples to ensure that all proteins are in same orientation D. Requires large quantities of protein to dtermine structure (Typicaly 5-10 ml of 1 mg/ml) E. The raw data obtained by Cryo-EM are 2D images of multiple frozen protein particles.
As you have seen, the protein assay relies upon the ability of proteins to bind the dye. Some substances such as dish soap can inhibit the interaction of the dye with the protein. If your unknown samples were accidentally analyzed using cuvettes that had not been well rinsed after washing, how would your calculated protein concentration be affected (Higher, Lower, No Change)? Briefly explain your reasoning.
Compare and contrast the following protein characterization techniques in terms of the principles governing their functions. affinity chomotagraphy vs hydrophobic interaction chromatography

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