please answer asap Q1: Protein Structure Matching: Match each term with its correct definition.Primary StructureSecondary StructureTertiary StructureQuaternary StructureA. Full 3D structure of a polypeptideB. Two or more polypeptides forming a complexC. a (alpha)-helices and ß (beta)-sheetsD. Amino acid sequence of a polypeptide

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Answered: Q1: Protein Structure Matching: Match…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Page 1 > of 3 ZOOM B. Propose une Toie onsuinin Teguiaung Dioou giucose concentrauon. Question 2: Label the protein structure level on lines 1,2,3, and 4 and label/describe the structure to which each box corresponds. Describe the characteristics of each structural level in the boxes below. MacBook Air DII 80 888 F10 F7 FB F5 F4 F3 * & # $ 7 8 3 4 E R T Y K F M C V .. .. この * 00 B
Discuss the different structures of protein. What are the five factors that promote protein folding and stability. Explain your answers in depth and detail.
Match the protein structure terms on the left with the descriptions on the right. v (Choose ) commonly observed combinations of secondary structural elements tertiary structure Long segments of secondary structure. supersecondary structure basic component of quaternary structure Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptide Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chain compact structural or functional regions within a given polypeptide functional structures formed by non-covalent interactions between multiple polypeptides. domain (Choosel subunit quaternary structure (Choose)
Protein Structure and Folding:a. Explain how changes in a protein’s amino acid sequence can change the way it behaves in water.b. Explain how changes in a protein’s amino acid sequence can change the way it interacts with othermolecules.c. Explain how changes in a protein’s amino acid sequence can change the way it forms secondary andtertiary structures when placed in water.
What is the major difference between tertiary and quaternary protein structure? The sequence of amino acids involved. The involvement of R (radical) groups. The number of polypeptides involved.
On 4. Below is a polypeptide with an unknown number of amino acids. On the diagram below: a. Circle EVERY peptide bond b. Circle and number each amino acid from 1, 2, 3, and so on; from left to right c. Label each amino acid as polar, non-polar, or electrically charged d. Label the N-terminus and C-terminus e. Select three pairs of amino acids that could potentially interact to influence tertiary structure AND state the bond/force/interaction type involved in each pair. H₂N-CH-C-N-CH-C- CH₂ CH₂ CH₂ NH CINH NH₂ Accessibility: Investigate CH₂ -NH -CH-C-N- CH-OH CH3 -CH-C-N CH₂ CH₂ -N- OH CHIC-OH CH₂ OH
Select the true statements about protein secondary structure. In an a-helix, the side chains are located on the outside of the helix. The secondary level of protein structure refers to the spatial arrangements of short segments of the protein. In a B-pleated sheet, the side chains are located between adjacent segments. Peptide bonds stabilize secondary structure. The x-helix is held together by hydrogen bonds between the amide N-H and C=O groups. Incorrect
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?
Discuss using your own words and illustrations the organisation of a protein, from its linear amino acid sequence, to its final three–dimensional configuration, which may include one or more polypeptides. Include what types of bonds help to stabilise each structural level, from primary through quaternary structure.
In your own words discuss the different structures (primary, secondary, tertiary, and Quaternary structures) of protein. What are the five factors that promote protein folding and stability. (Hint: One factor is the Hydrogen bond). Extra Hint: Another factor is the Hydrophobic effect. Do not just copy and paste from other sources/websites/books/articles/etc.
Structure Writing: Draw the structure of peptide with sequence G-A-N-D-A
Prepare & define the alpha-helical structure of protein with examples

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