Chapter 2: Problem 8
Bonding between atoms within an enzyme such as trypsin is best described as A peptide. B. saccharide. C. ionic. D. van der Waals.
Short Answer
Expert verified
A. peptide.
Step by step solution
01
Understand the Question
The question asks about the type of bonding between atoms within an enzyme specifically, such as trypsin.
02
Analyze the Options
Examine the different types of bonds listed in the options: peptide, saccharide, ionic, and van der Waals.
03
Recall the Structure of Enzymes
Enzymes are proteins, and proteins are made up of amino acids connected by specific bonds.
04
Identify the Bond Type in Proteins
Proteins, including enzymes like trypsin, are held together by peptide bonds, which connect amino acids.
05
Choose the Correct Answer
Based on the analysis, the best description of the bonding between atoms within an enzyme like trypsin is peptide bonds.
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Key Concepts
These are the key concepts you need to understand to accurately answer the question.
Peptide Bonds
Peptide bonds are the connections between amino acids in a protein. They are a type of covalent bond and are formed through a dehydration reaction, where a water molecule is removed. In this reaction, the carboxyl group of one amino acid links to the amino group of another. Peptide bonds are strong and stable, which is crucial for maintaining the integrity of proteins and their functions within living organisms.
Amino Acids
Amino acids are the building blocks of proteins. Each amino acid has a basic structure consisting of an amino group (NH2), a carboxyl group (COOH), a hydrogen atom, and a distinct side chain (R group) all attached to a central carbon atom. There are 20 different amino acids found in proteins, each with unique side chains that confer different properties. Proteins are formed by linking amino acids together via peptide bonds to form chains, which then fold into complex structures required for biological functions.
Protein Structure
Proteins have four levels of structure. The primary structure is the sequence of amino acids linked by peptide bonds. The secondary structure involves alpha-helices and beta-pleated sheets formed by hydrogen bonding between the backbone atoms. The tertiary structure is the overall 3D shape of a single protein molecule, stabilized by various interactions, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges. Quaternary structure refers to the arrangement of multiple protein subunits into a larger complex. Each level is crucial for the protein's final shape and function.
Enzymatic Function
Enzymes are proteins that act as biological catalysts. They speed up chemical reactions by lowering the activation energy required. Enzyme function depends on the protein's structure, particularly the active site where substrates bind. The specificity of enzymes is due to their unique 3D structures, which are determined by the sequence of amino acids and the peptide bonds that link them. Changes in the enzyme's environment, such as pH or temperature, can affect its shape and efficacy.