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
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
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
If your molecule C4H11N5 was the side chain of an amino acid, in a protein, what tertitary structure stabilizers could be present? Make a key and use colors to highlight what part of your structure can be stabilized in each manner?
One of the most advanced methods for determining a protein sequence is tandem mass spectrometry (MS/MS). Select from the list of statements below all that applies to MS/MS. Group of answer choices CID is one way of performing tandem MS experiments The experiment start by chopping the protein into smaller peptide fragments using an enzyme These peptide fragments are later introduced into the mass spectrometer to determine their molecular weight Peptide fragments are selected for further fragmentation by collision with an inert gas There are only 4 types of ions which can result from MS/MS fragmentation: a, b, x, and y ions The a and b ions are the ones with the original C terminus, whereas the x and y ions are the ones with the original N-terminus All of the above
Relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10-5and 10-8M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 103and 105M, respectively. Which protein has the highest affinity for ligand X? Explain your reasoning.
Although the bond energy for the hydrogen bond in a vacuum is estimated to be about 20 kJ/mol, we find that each hydrogen bond in a folded protein contributes much less--probably less that 5 kJ/mol--to the enthalpy of protein stabilization. Suggest an explanation for this difference. Explain briefly.
The amino acid histidine has ionizable groups with pKa values of 1.8, 6.0, and 9.2, as shown. COOH H₂N-CH CH₂ H 2 -N H lonizable group 6.0 1.9 7.94 0.11 N H CH -COOH H₂N-CH | CH₂ H 2 N 1.8 COO- I pk₁ C H COO- CH -HisH+ H₂N-CH 6.0 COO- pk ₂. CH₂ H 2 H -His N CH COO™ H₂N-CH 9.2 pk 3 CH₂ H -N с H —NH — —NH, A biochemist makes up 95 mL of a 0.11 M solution of histidine at a pH of 5.1. She then adds 60 mL of 0.10 M HCI. What is the pH of the resulting solution? N CH
For alanine, Ka1=5.1105,Ka2=1.81010 . Calculate the ratios [Z]/[C+] and [Z]/[A+] at pH (a) 2.00. (b) 6.00. (c) 10.50. What is the principal species at each pH?
A 1.00-mg sample of a pure protein yielded on hydrolysis 0.0165 mg of leucine and 0.0248 mg of isoleucine. What is the minimum possible molar mass of the protein? (MMleucine=MMisoleucine=131g/mol)