4. Course Code: BIO-121 Chapter 3: Molecules of Life Course Name: Principles Of Biology-1 Protein's function depends on its 3D shape. High temperature may result in protein denaturation. (i) Explain what is meant by "denatured". (ii) Explain why a protein may not be functional if it is denatured. (iii) Other than temperature, list the factors that can result in protein denaturation.

4. Course Code: BIO-121 Chapter 3: Molecules of Life Course Name: Principles Of Biology-1 Protein's function depends on its 3D shape. High temperature may result in protein denaturation. (i) Explain what is meant by "denatured". (ii) Explain why a protein may not be functional if it is denatured. (iii) Other than temperature, list the factors that can result in protein denaturation.

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Topic: ISOLATION AND CHARACTERIZATION OF PROTEINS 1. Which amino acids contains the following:a. Sulfur/sulfhydryl groupb. Aromatic groupc. Imidazole ringd. Guanidine groupe. Indole ring2. Classify the following proteins to their biological functions (casein, albumin, gluten, andmyoglobin) 3. Which level of protein structure organization are lost hydrolysis and denaturation?4. What is the Beer-Lambert’s Law? Why is it relevant to the quantitative analysis of proteins?
The elegance and importance of proper protein folding and assembly cannot be overstated. Simple electrostatic interactions are fully responsible for long peptide chains becoming giant, globular, functional proteins. Research and discuss two examples of improper protein folding. What is the cause of each malformed protein? What is the consequence of this deformity? What are potential treatment options, and how do they address and remedy the problem?
8. Multiple choice. Which of the following is not a method that can be used to determine the 3° structure of proteins? (2 pts) a) Protein X-ray crystallography b)) Circular dichroism c) Cryogenic electron microscopy d) Protein NMR 9. Multiple choice. Approximately what overall yield can you expect from the solid phase peptide synthesis (SPPS) of a "10-mer" (a 10 amino acid peptide), if the yield from each step is 85%? (2 pts) 23% b) 20% c) 85% d) 71% 10. Multiple choice. Which protein purification method is best for an experiment in which you want to purify a monomeric form of a protein away from a tetrameric form? (2 ptrs) (-His a) Affinity chromatography S b) High pressure liquid chromatography c) lon exchange chrommatography d) Size exclusion chromatography 2. I1. Short answer. What is the Edman degradation experiment useful for? (3 pts) purdinate an for prry structers steps .
offset=next&assignment ProblemID=218423920 Which of the following statements is FALSE regarding proteins? The three-dimensional shape of a protein is critical for the functioning of that protein. O There is a link between improperly folded proteins and disease in both mad cow disease and Alzheimer's disease. Alzheimer's disease causes proteins in the brain to become improperly folded. O High heat and a change in pH can denature a protein. Submit Part C Request Answer Why does the story in the video start in Colombia? <
Reminder : ONLY ONE GRAPH
Part C - Exploring antiparallel 3 sheet structure The hydrogen bonding between antiparallel sheets, also visible in the pdb by selecting the antiparallel sheet view, is shown. Locate the N- and C-termini in this image. Select the antiparallel sheet view in the pdb file. How many peptide chains are shown? O 1 O 2 3 O 4 Submit Request Answer
Is there more than one subunit shown? Is your protein bound to anything else? Describe the secondary structures you see.
Part I. Protein structure You have the toy model for a protein in the water (W) environment of the cell shown. a) How many residues (amino acids) does this toy protein have? b) How many hydrophobic (H), hydrophilic (P), and charged (C) residues are there? c) Sketch the molecule on your answer sheet and then show the positions of the favorable C-C (charge-charge) interactions on the figure.
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Rationalize the following observations.(a) Serine is the amino acid residue that can be replaced with theleast effect on protein structure and function.(b) Replacement of tryptophan causes the greatest effect on protein structure and function.(c) Replacements such as Lys -> Arg and Leu -> Ile usually havevery little effect on protein structure and function.
H8. Protein A interacts with biomolecule B and forms a complex AB, with a dissociation constant KD = 1 µM at 25 °C, (for dissociation, AB ⇋ A + B, KD=[A][B]/[AB]). The interface contains a phenylalanine residue. A biochemist mutated the phenylalanine of protein A to a tyrosine (A’), which introduced a hydrogen bond between the hydroxyl group of the tyrosine with B without affecting any other interactions. The formation of the hydrogen bond releases a heat at 11.4 kJ/mol. What is the KD of the complex of the mutant A’ with B? Hint: Gas constant R = 8.3145 J/K/mol, Euler’s number e = 2.7183, ln(A) - ln(B) = ln(A/B).
Problem: From the following information determine the amino acid sequence of a peptide. N-terminal Edman gives PTH-Alanine C terminal carboxypeptidase treatment, no observable reaction Trypsin cleavage gives three products Arg Peptide containing Ala, Lys Peptide containing Asp, Met, Phe, Pro Mild Chymotrypsin cleavage gives 2 peptides Peptide containing Asp, Pro Peptide containing Ala, Arg, Lys, Met, Phe CNBr cleavage gives 2 peptide Peptide containing Ala, Arg, Lys and homoserine Peptide containing Asp, Phe, Pro You must supply the answer as the 3-letter amino acid sequence from N-terminus to C-terminus in the form (you must use dashes, not spaces between the amino acids)