WRITING EQUATIONS USING MOLECULAR STRUCTURES DIRECTION: Given the following biomolecules below, write the DENATURATION SYNTHESIS OF PROTEIN using molecular structures with the required number of units. You can write either horizontal or vertical position. Dehydration synthesis of protein with 3 units

WRITING EQUATIONS USING MOLECULAR STRUCTURES DIRECTION: Given the following biomolecules below, write the DENATURATION SYNTHESIS OF PROTEIN using molecular structures with the required number of units. You can write either horizontal or vertical position. Dehydration synthesis of protein with 3 units

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section3.1: Carbon Atoms And Organic Molecules

Problem 3C

See similar textbooks

Similar questions

Biochemists talk about protein structure at four distinct levels: primary, secondary, tertiary and quaternary structure. Below are depictions of each of these levels of protein structure. For each image, match the term and the written description of the level of protein structure that the image depicts. Drag the appropriate items to their respective bins.
Explain Four Levels of Protein Structure with examples and talk about the importance of each structure (Primary, Secondary, Tertiary, and Quaternary structure). With photos please
Predict the protein 3° structure of the following protein sequence. Provide detail from 2° structure principles Nterm – SLDVTFSPGAEITFKWNPGSFNSLKDTIRQVTDK – Cterm
The addition of ethanol, CH3CHOH, t an aqueous solution lowers the surface tension of the solution. Predict whether adding ethanol to an aqueous protein solution will tend to stabilize or unfold the protein. Briefly explain.
Denatured protein is in a low energy state. What sort of explanation can you use to rationalize that statement? Hint: consider Gibbs free energy.
Please answer the question below and show all your work. You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole^-1 cm^-1 Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20- fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution?
You have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most suitable technique (X-ray crystallography, NMR, cryo-EM) for structure determination of this protein? Explain your reasoning.
a 3d structure of protein with acces number of P02008 at uniprot database.
draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 and put each charges beside the amino acids then compute for the isoelectric point please show complete solution DFACKT
The twisted proteins store elastic potential energy as it twists or untwists from its equilibrium state. The energy function for this system is shown in the figure where the energy is given in multiples of kBT which is a unit of energy used by biochemists when working at the molecular level. (1.0 kBT = 4.11×10−21 J). Figure 6 shows a horizontal line at an energy level of 136 kBT , which gives a total angular range of 2.095 radians. If the energy level of the ATP-synthase stalk is 100 kBT instead, between what angles is the stalk confined? Explain your reasoning.
You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?
Which reagent(s) would you use for the following processes related to protein chemistry? Write the respective equations. a) Identification of the terminal amino residue. b) Determination of the amino acid sequence of the peptide Gly-Asp-Ala-Cys c) Reversible denaturation of a protein containing disulfide bonds d) Hydrolysis of peptide bonds of aromatic residues of a protein e) Fragmentation of a protein by breaking peptide bonds on the carbonyl side of methionines.