Myoglobin Secondary Structure Analysis Choose ONE of the following sequences from myoglobin and carry out the Secondary analysis for propensity for a-helix, ẞ-sheet and ẞ-turn VEADVAGHGQDILILRFK PLAQSHATKHKIPIKYLE LELFRKDIAAKYKELGYQG Compare the results of your analysis to the three-dimensional structure for the protein What structure do you predict? Does it match the actual secondary structure seen in the protein? If not, can you suggest why not?

Myoglobin Secondary Structure Analysis Choose ONE of the following sequences from myoglobin and carry out the Secondary analysis for propensity for a-helix, ẞ-sheet and ẞ-turn VEADVAGHGQDILILRFK PLAQSHATKHKIPIKYLE LELFRKDIAAKYKELGYQG Compare the results of your analysis to the three-dimensional structure for the protein What structure do you predict? Does it match the actual secondary structure seen in the protein? If not, can you suggest why not?

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 22.68P

See similar textbooks

Similar questions

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)
22-49 Based on your knowledge of the chemical properties of amino acid side chains, suggest a substitution for leucine in the primary structure of a protein that would probably not change the character of the protein very much.
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…
Describe two examples of protein folding patterns and identify what level of protein structure they belong to. What other reagents might you use besides ferric chloride to test affinity for metal ions? How many grams of the protein are in one 200 g glass of milk?
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 use of salt bridges or hydrophobic interactions (or pockets) to stabilize interactions between more distant amino acids within a single polypeptide, is a demonstration of protein TERTIARY structure. True False
What amino acid is found at this position: 148 of 4ALD? Explain why this position in your protein is important and outline the effects the mutation will have on the 3D structure and the function of your protein ( 4ALD).
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
The carbon-nitrogen peptide bond is rigid, but rotation can take place about the N-C and the Co-C bonds in a protein (Co is the a carbon atom). These bond angles define the conformation of the peptide chain. Consider the Ramachandran plot to answer both questions. Which observation most likely describes part of an observed a helix? p = +60°; y +40°; many Gly residues = -60°; y = −47°; many Ala residues = = -57°; y = −47°; many Pro residues = -140°; y = +130°; many Val residues p = -59°; y = +150°; many Ser residues Which observations would not likely occur in a ẞ sheet? p = +60°; y = +60°; many Gly residues p = −57°; y = −49°; many Ala residues = -120°; y = +120°; many Tyr residues = -51°; y = +153°; many Gly and Pro residues p = −139°; y = +135°; many Val residues (degrees) 180 120 60 0 -60 -120 -180 -180 0 (degrees) 180
5 ased on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 97.4 kDa and 47.2 kDa, what can be said about the number and size of the protein monomers, as well as the nature of the bonds holding together the complete quaternary structure of the proteins?
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…