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Please provide explanations and work for each part of the question. If able to keep the same format of the question - the table with the answers within along with explanations - that would be the best case. This is biochemistry. Thank you

Please provide explanations and work for each part of the question. If able to keep the same format of the question - the table with the answers within along with explanations - that would be the best case. This is biochemistry. Thank you

Biochemistry
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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Please provide explanations and work for each part of the question. If able to keep the same format of the question - the table with the answers within along with explanations - that would be the best case. This is biochemistry. Thank you

A major difference between protein and DNA is that DNA has the same double-stranded structure no matter what the content or order of the nitrogenous bases, but proteins have a different shape depending on the content and order of the amino acids. Evolution has led to proteins that fold into precise shapes, whether globular, tubular, fibrous, spherical, or netlike, based on how the polypep- tide chain folds. It folds a bit at a time, making and breaking molecular interactions as it folds. To describe these shapes, the four levels of protein structure were named primary, secondary, tertiary, and quaternary. The interactions formed in a protein as it is synthesized and then as it folds are the peptide bond, the hydrogen bond, ionic bonds, polar interactions, disulfide bonds, and hydrophobic interactions. In the following chart, match each level to the interaction types that form it and to the protein motifs or features generally ascribed to it. The possible interaction types and motifs to choose from are listed in the boxes following the chart. LEVEL Primary Secondary Tertiary Quaternary Interaction Types ■ Disulfide bond Hydrogen bond Hydrophobic interaction ▪ lonic bond Peptide bond Polar interaction INTERACTION TYPE MOTIF/FEATURE ASCRIBED TO THAT LEVEL Motif/Features Ascribed . a-helix . B-sheet ▪ B-turn . Barrel . Fold ▪ Hexameric structure . Overall 3D shape ■ Polypeptide chain . Protein domain • Tetrameric enzyme
Transcribed Image Text:A major difference between protein and DNA is that DNA has the same double-stranded structure no matter what the content or order of the nitrogenous bases, but proteins have a different shape depending on the content and order of the amino acids. Evolution has led to proteins that fold into precise shapes, whether globular, tubular, fibrous, spherical, or netlike, based on how the polypep- tide chain folds. It folds a bit at a time, making and breaking molecular interactions as it folds. To describe these shapes, the four levels of protein structure were named primary, secondary, tertiary, and quaternary. The interactions formed in a protein as it is synthesized and then as it folds are the peptide bond, the hydrogen bond, ionic bonds, polar interactions, disulfide bonds, and hydrophobic interactions. In the following chart, match each level to the interaction types that form it and to the protein motifs or features generally ascribed to it. The possible interaction types and motifs to choose from are listed in the boxes following the chart. LEVEL Primary Secondary Tertiary Quaternary Interaction Types ■ Disulfide bond Hydrogen bond Hydrophobic interaction ▪ lonic bond Peptide bond Polar interaction INTERACTION TYPE MOTIF/FEATURE ASCRIBED TO THAT LEVEL Motif/Features Ascribed . a-helix . B-sheet ▪ B-turn . Barrel . Fold ▪ Hexameric structure . Overall 3D shape ■ Polypeptide chain . Protein domain • Tetrameric enzyme
Expert Solution
Step 1: Protein structure

Protein structure is a fundamental concept within biochemistry, encompassing the hierarchical arrangement of proteins across four key levels: primary, secondary, tertiary, and quaternary. Each of these levels plays a vital role in determining a protein's functionality and structural conformation.

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