Mass spectrometry X-ray diffraction Both techniques Answer Bank protein may be denatured small amounts of protein are sufficient can detect a covalent modification to a protein requires a large amount of protein analysis requires information about the protein-coding gene or genes protein sample must be pure protein must be conformationally stable Mass Spectrometry and x-ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to MS, X-Ray, or both.

Mass spectrometry X-ray diffraction Both techniques Answer Bank protein may be denatured small amounts of protein are sufficient can detect a covalent modification to a protein requires a large amount of protein analysis requires information about the protein-coding gene or genes protein sample must be pure protein must be conformationally stable Mass Spectrometry and x-ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to MS, X-Ray, or both.

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter22: Proteins

Section: Chapter Questions

Problem 22.52P

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True or false and why is false 8 Structures produced by X-ray diffraction are as good as the solutions from which they are derived 9 Hard keratins (such as in the skin) are less resistant to stretch because the larger number of disulfide bonds resist deformative forces. 10 The vast majority of structures deposited in the Protein Databank (>95%) have been determined using NMR
The image below is a positive ionization mode Electrospray ionization-mass spectrum (ESI-MS) spectrum for a peptide, obtained using high resolution mass spectrometry. If ionization occurs through de-protonation (assuming that the mass of a proton is 1.0 Da), what is the neutral mass of the peptide, in Da? 627.271 627.604 100 - 627.938 628.271 628.604 628.938 627.0 628.0 629.0 mass/charge (m/z) 628.271 626.271 1878.813 O 1884.813 % Abundance
protein backbone for any amino acid residues from exercise 4 that are capable. 6. For each of the following representations (from OpenStax Biology), indicate whether it is describing primary, secondary or tertiary protein structure a. OHH R HA RICH OHH R OHH R OHH C-NCC-NCC-NCC-NCC-N H H R HH A A R RHHO R CCN_C_CON HHO CCN-C CON-C CN-C HH C=O HITIR HF RH HO R H CN-CCN-C CN-C CN-C CN-C RE H-N RICH Q=0 b. Gly Ser His Leu Val Glu Ala Leu Tyr Leu Val as SC.
What are two ways to measure the total amount of all proteins in a purification sample? O 1) Calculating the yield and 2) calculating the purity of a purification. O 1) Measuring absorbance at 280 nm and 2) using an enzymatic assay for your protein of interest. O 1) Quantitating the amount of your protein of interest using binding of a labeled antibody (e.g.. an ELISA) and 2) using a dye-binding assay. O 1) Measuring absorbance at 280 nm and 2) using a dye-binding assay.
macollege.instructure.com/courses/352/pages/covid-proteins-lab-manual?module_item_id=D44333 A = abc Where "A" is absorbance, "a" is molar absorptivity, "b" is the path length (length of the cuvette in units of cm), and "c" is concentration (mol/L). The molar absorptivity is an intrinsic property of a molecule which tells us how intensely it will absorb at a particular wavelength. If "A" is a unitless quantity, "b" is in units of cm, and "c" is in units of mol/L, then what are the units of molar absorptivity? Do a little research to learn how alpha-helices and beta-sheets are drawn in protein structures. If most of the absorption properties are coming from the alpha-helices in these proteins, and many alpha-helices have similar absorbance properties across different proteins, which protein would you predict would have the highest molar absorptivity? Your job is to use the following data table to determine the molar absorptivity for each of the following proteins at their respective…
Use the online JPRED 4 secondary structure prediction tool (Pred: A Protein Secondary Structure Prediction Server (dundee.ac.uk) to predict the secondary structure for the following input sequence: MNLVLMGLPGAGKGTQAEKIVAAYGIPHISTGDMFRAAMKEGTPL GLQAKQYMDRGDLVPDEVTIGIVRERLSKDDCQNGFLLDGFPRTV AQAEALETMLADIGRKLDYVIHIDVRQDVLMERLTGRRICRNCGAT YHLIFHPPAKPGVCDKCG GELYQRADDNEATVANRLEVNMKQMK PLVDFYEQKGYLRNINGEQDMEKVFADIRELLGGLAR How many helical regions are predicted? (Hint: see the View Simple Results in HTML). A 4 B 6 C O D 8 E 1
Question 2. While internal cysteine amino acid sidechains in proteins undergo oxidation to produce disulfide crosslinks that stabilize the protein structure after folding, solvent-exposed cysteine sidechains can remain in their reduced thiol form and serve as reactive nucleophiles (recall for instance Acyl Carrier Proteins involved in fatty acid biosynthesis or various oxidoreductase enzymes). The reactive thiol groups in proteins can be detected using Ellman's test, wherein the protein is reacted with a disulfide Ellman's reagent to form a new mixed disulfide and a 2-nitro-5-thiobenzoate (TNB) byproduct. Upon addition of base, TNB is deprotonated to form a dianion, which absorbs light in the visible region and can be detected using UV-Vis spectroscopy. Ellman's Reagent CO₂H -NO₂ internal disulfide crosslink O₂N- HO₂C SH solvent- exposed thiol UV Absorbance at 412 nm O₂N- -S TNB²- alkaline pH O₂N- SH HO₂C 2-nitro-5-thiobenzoate (TNB) -NO2 mixed disulfide CO₂H a) Provide a detailed…
Answer in step by step with explanation. Don't use Ai and chatgpt.
About a decade ago, it was more common to use peptide mass mapping to identify a protein cut from a gel. Peptide mass mapping involves digesting the protein with trypsin and then measuring the peptide masses using MALDI-TOF mass spectrometry. The more superior method of identifying a protein from a gel is to digest the protein with trypsin and then use liquid chromatography to separate the peptides. The separated peptides are then electrosprayed into a tandem mass spectrometer. The MS-MS data is uploaded into a database such as MASCOT for protein identification. Explain why the LC-MS-MS method is superior to the peptide mass mapping method.
Of the following methods listed below, which could not be used to obtain a reasonable estimate of the molecular mass of a monomeric protein? Select all that apply. O Electrospray ionization mass spectrometrylsoelectric focusing O Gel filtration O All of these methods could be used O Isoelectric focusing O Sodium dodecyl sulfate polyacrylamide gel electrophoresis O Total amino acid sequence determination by Edman degradation
Use the values provided below to calculate the predicted isoelectric point, pl, value for aspartame. HO NH2 NH2 phenylalanine aspartic acid pКа1 а-СООН%3D 1.83 pKa2 a-NH3* = 9.13 pКa1 а-СООН %3D 1.88 pKa2 a-NH3* = 9.60 pKa3 side chain-COOH = 3.65 %3D
The amino acid histidine has ionizable groups with pKą values of 1.8, 6.0, and 9.2, as shown. COOH T H₂N-CH | CH₂ H -O pH UT = ZI Ionizable -COOH group CH H₂N-CH T 1.8 COO- pk₁ CH2 UI COO™ H IZ CH -HisH+ COO™ + H₂N-CH 6.0 pK₂ CH ₂ UI -His H CH -NH COO™ H₂N-CH 9.2 pk3 CH ₂ UI —NH₂ H A biochemist makes up 80 mL of a 0.11 M solution of histidine at a pH of 5.1. She then adds 60 mL of 0.10 M HCl. What is the pH of the resulting solution? CH