Biomolecules: Proteins Fundamentals Quiz

<p>Between two cysteine monomers</p> Signup and view all the answers

<p>The three-dimensional arrangement of a single polypeptide chain</p> Signup and view all the answers

<p>The arrangement of multiple polypeptide chains in a protein</p> Signup and view all the answers

<p>Spontaneously</p> Signup and view all the answers

<p>By molecular chaperones, which bind to exposed and unfolded regions</p> Signup and view all the answers

<p>A single point mutation resulting in a change in the amino acid sequence and the formation of sickle-shaped red blood cells</p> Signup and view all the answers

<p>Loss of a protein's three-dimensional structure and biological activity</p> Signup and view all the answers

<p>The side chains (R groups)</p> Signup and view all the answers

<p>Functional groups like alcohols and amines</p> Signup and view all the answers

<p>20</p> Signup and view all the answers

<p>Sequence of amino acids joined by peptide bonds</p> Signup and view all the answers

<p>$ ext{Hydrogen bonding}$</p> Signup and view all the answers

<p>Tertiary structure</p> Signup and view all the answers

<p>Alpha helices and beta pleated sheets</p> Signup and view all the answers

<p>Secondary structure</p> Signup and view all the answers

<p>Different polypeptide chains or regions of the same chain that have turned back on themselves</p> Signup and view all the answers

<p>Tertiary structure</p> Signup and view all the answers

<p>Amino acids</p> Signup and view all the answers

<p>Approximately 100,000</p> Signup and view all the answers

<p>Catalyzing metabolic processes</p> Signup and view all the answers

<p>Distinctive side chain or R group</p> Signup and view all the answers

<p>$\beta$-peptide bond</p> Signup and view all the answers

<p>Central Carbon and Hydrogen</p> Signup and view all the answers

<p>A distinctive side chain or R group</p> Signup and view all the answers

<p>Non-covalent bond</p> Signup and view all the answers

<p>Different polypeptide chains</p> Signup and view all the answers

<p>Secondary structure</p> Signup and view all the answers

<p>Non-polar side chains</p> Signup and view all the answers

<p>$\alpha$-amino acids and peptide bonds</p> Signup and view all the answers

<p>Stabilizing the protein structure</p> Signup and view all the answers

<p>20</p> Signup and view all the answers

<p>Side chains (R groups)</p> Signup and view all the answers

<p>Hydrogen bond</p> Signup and view all the answers

<p>Assisting in the folding of newly synthesized proteins to their functional conformation</p> Signup and view all the answers

<p>Catalyzing metabolic processes</p> Signup and view all the answers

<p>Distinctive side chain or R group</p> Signup and view all the answers

<p>Arrangement of multiple folded protein subunits into a functional macromolecule</p> Signup and view all the answers

<p>Hydrogen bonds between amino acids in a polypeptide chain</p> Signup and view all the answers

<p>Variations in the sequence and arrangement of amino acids within the polypeptide chain</p> Signup and view all the answers

<p>Disruption of a protein's native conformation due to changes in pH or temperature</p> Signup and view all the answers

<p>Oxidative coupling between two cysteine residues</p> Signup and view all the answers

<p>Three-dimensional arrangement of all atoms in a single polypeptide chain</p> Signup and view all the answers

<p>Assisting in correct folding and preventing misfolding or aggregation</p> Signup and view all the answers

<p>Hydrophobic interactions</p> Signup and view all the answers

<p>Disulfide bond</p> Signup and view all the answers

<p>Point mutation</p> Signup and view all the answers

<p>Secondary structure</p> Signup and view all the answers

<p>Carbonyl groups in the polypeptide backbone</p> Signup and view all the answers

<p>By chaperone proteins</p> Signup and view all the answers

<p>Van der Waals interactions</p> Signup and view all the answers

<p>Covalent bonding</p> Signup and view all the answers

<p>The arrangement of multiple polypeptide chains in a protein</p> Signup and view all the answers

<p>By molecular chaperones binding to exposed and unfolded regions</p> Signup and view all the answers

<p>Loss of three-dimensional structure and biological activity</p> Signup and view all the answers

<p>Side chain properties</p> Signup and view all the answers

<p>Biological catalysis</p> Signup and view all the answers

<p>Side chain interactions</p> Signup and view all the answers

<p>Characteristic of tertiary structure</p> Signup and view all the answers

<p>Side chain properties</p> Signup and view all the answers

<p>Catalyzing metabolic processes</p> Signup and view all the answers

<p>Distinctive side chain or R group</p> Signup and view all the answers

<p>Peptide bond</p> Signup and view all the answers

<p>$ ext{~}100,000$</p> Signup and view all the answers

<p>Unfolding of a protein from its native state</p> Signup and view all the answers

<p>Van der Waals interactions</p> Signup and view all the answers

<p>Interactions among R groups</p> Signup and view all the answers

<p>Through covalent bonding between two cysteine residues' carboxylic acid groups</p> Signup and view all the answers

<p>Interactions among R groups</p> Signup and view all the answers

<p>Abnormalities in hemoglobin synthesis</p> Signup and view all the answers

<p>Side chains containing pure hydrocarbon alkyl groups or aromatic rings</p> Signup and view all the answers

<p>20</p> Signup and view all the answers

<p>Stabilizing the secondary structure of proteins</p> Signup and view all the answers

<p>Secondary structure</p> Signup and view all the answers

<p>They have hydrogen bonding between amino acids in the same chain, forming a spiral structure</p> Signup and view all the answers

<p>Different polypeptide chains or regions of the same chain that have turned back on themselves</p> Signup and view all the answers

<p>The side chains (R groups)</p> Signup and view all the answers

<p>Tertiary structure</p> Signup and view all the answers

<p>Central carbon bonded to a hydrogen atom, an amino group, a carboxyl group, and a variable R group</p> Signup and view all the answers

<p>The specific conformation formed by polypeptide chains affecting the protein's function</p> Signup and view all the answers

<p>Protein structure and stability are influenced by a variety of interactions. Hydrophobic interactions occur between nonpolar R groups, van der Waals interactions are weak electric forces between neutral molecules, and covalent bonds, specifically disulfide bonds, are the strongest interactions in proteins.</p> Signup and view all the answers

<p>In vitro, a protein can spontaneously fold and adopt its functional conformation. In vivo, proteins are assisted in folding by molecular chaperones, which bind to exposed and unfolded regions, aiding in the correct folding process.</p> Signup and view all the answers

<p>The quaternary structure refers to the arrangement of multiple polypeptide chains in a protein. An example is hemoglobin, which consists of four polypeptide chains (two alpha and two beta).</p> Signup and view all the answers

<p>Proteins act as enzymes, which are biological catalysts that speed up chemical reactions. Enzymes are specific to certain reactions and have a unique shape to interact with their substrates. They are not changed by the reaction they catalyze and can be reused.</p> Signup and view all the answers

<p>Denaturation refers to the loss of a protein's three-dimensional structure and biological activity. Proteins can be denatured by changes in temperature, chemical exposure, or pH, leading to a loss of biological activity.</p> Signup and view all the answers

<p>Proteins have different functions based on their structure and domains. The tertiary structure of a protein refers to the three-dimensional arrangement of a single polypeptide chain, which contributes to its specific function.</p> Signup and view all the answers

<p>Sickle cell anemia is caused by a single point mutation, resulting in a change in the amino acid sequence and the formation of sickle-shaped red blood cells. This alters the shape of the red blood cells and affects their ability to carry oxygen.</p> Signup and view all the answers

<p>Disulfide bridges form between two cysteine monomers in a protein through the oxidation of sulfhydryl groups. These covalent bonds contribute to the protein's stability and structure.</p> Signup and view all the answers

<p>In vivo, proteins are assisted in folding by molecular chaperones, which bind to exposed and unfolded regions, aiding in the correct folding process and preventing misfolding or aggregation.</p> Signup and view all the answers

<p>Proteins have different levels of structure including primary, secondary, tertiary, and quaternary structures. The primary structure refers to the linear sequence of amino acids, while the secondary structure involves local folding patterns such as alpha helices and beta sheets. The tertiary structure refers to the three-dimensional arrangement of a single polypeptide chain, and the quaternary structure involves the arrangement of multiple polypeptide chains in a protein.</p> Signup and view all the answers

<p>Proteins are macromolecules composed of amino acids.</p> Signup and view all the answers

<p>Approximately 100,000 different proteins in the human body.</p> Signup and view all the answers

<p>Molecular chaperones assist in the proper folding of proteins during synthesis.</p> Signup and view all the answers

<p>Most enzymes are important for catalyzing metabolic processes in the body.</p> Signup and view all the answers

<p>The distinctive side chain or R group of each amino acid gives it unique characteristics and identity.</p> Signup and view all the answers

<p>Enzymes play a crucial role in catalyzing metabolic processes in the body.</p> Signup and view all the answers

<p>Structural and functional domains contribute to the overall tertiary structure and function of proteins.</p> Signup and view all the answers

<p>All amino acids have a central carbon and hydrogen, an amino functional group, and a carboxylic acid functional group or carboxylate.</p> Signup and view all the answers

<p>Proteins are major structural components of cells and are essential for growth, repair, and maintenance of the cell.</p> Signup and view all the answers

<p>The primary purpose is to provide an understanding of the fundamentals of human biology, including biomolecules such as proteins.</p> Signup and view all the answers

<p>Polar side chains contain functional groups like acids, amides, alcohols, and amines which make the amino acid hydrophilic, while non-polar side chains contain pure hydrocarbon alkyl groups or aromatic rings which make the amino acid hydrophobic.</p> Signup and view all the answers

<p>The four levels of protein organization are primary, secondary, tertiary, and quaternary. The primary structure refers to the sequence of amino acids joined by peptide bonds. The secondary structure involves repeating patterns formed by hydrogen bonding between amino acids, such as alpha helices and beta pleated sheets. Tertiary structure is the three-dimensional shape of an individual polypeptide chain, determined by interactions among its R groups. Quaternary structure refers to the arrangement of multiple polypeptide chains in a protein.</p> Signup and view all the answers

<p>Hydrogen bonding plays a crucial role in protein structure and function by providing stability. It is a non-covalent bond between a hydrogen atom with a partial positive charge and an oxygen or nitrogen atom with a partial negative charge. Although weaker than covalent bonds, the numerous hydrogen bonds in a protein allow it to be stabilized.</p> Signup and view all the answers

<p>Alpha helices have hydrogen bonding between amino acids in the same chain, forming a spiral structure. Beta pleated sheets have hydrogen bonding between different polypeptide chains or regions of the same chain that have turned back on themselves, forming a sheet-like structure.</p> Signup and view all the answers

<p>Proteins have diverse functions, including catalyzing biochemical reactions (as enzymes), providing structural support, transporting essential molecules, and serving as signaling molecules.</p> Signup and view all the answers

<p>There are 20 commonly found amino acids in proteins. They are classified as polar, non-polar, acidic, and basic.</p> Signup and view all the answers

<p>The specific conformation of polypeptide chains affects the protein's function. The arrangement of the amino acids and their interactions determine the protein's overall structure and activity.</p> Signup and view all the answers

<p>The side chains (R groups) of amino acids determine their polarity and charge, with polar and non-polar side chains contributing to the hydrophilic or hydrophobic nature of the amino acid.</p> Signup and view all the answers

<p>The presence of alpha helices and beta pleated sheets, formed by hydrogen bonding between amino acids, contributes to the overall three-dimensional shape of proteins, influencing their stability and function.</p> Signup and view all the answers

<p>The main types of interactions involved in determining the tertiary structure of a protein are hydrogen bonding, disulfide bridges, hydrophobic interactions, and van der Waals forces.</p> Signup and view all the answers

<p>amino acids</p> Signup and view all the answers

<p>proteins</p> Signup and view all the answers

<p>proteins</p> Signup and view all the answers

<p>identity</p> Signup and view all the answers

<p>bond</p> Signup and view all the answers

<p>synthesis</p> Signup and view all the answers

<p>body</p> Signup and view all the answers

<p>chains</p> Signup and view all the answers

<p>protein</p> Signup and view all the answers

<p>Denaturation</p> Signup and view all the answers

<p>enzymes</p> Signup and view all the answers

<p>reactions</p> Signup and view all the answers

<p>catalyze</p> Signup and view all the answers

<p>denatured</p> Signup and view all the answers

<p>bonds</p> Signup and view all the answers

<p>functions</p> Signup and view all the answers

<p>mutation</p> Signup and view all the answers

<p>side chains</p> Signup and view all the answers

<p>basic</p> Signup and view all the answers

<p>hydrophilic</p> Signup and view all the answers

<p>hydrophobic</p> Signup and view all the answers

<p>proteins</p> Signup and view all the answers

<p>function</p> Signup and view all the answers

<p>quaternary</p> Signup and view all the answers

<p>peptide bonds</p> Signup and view all the answers

<p>sheets</p> Signup and view all the answers

<p>stabilized</p> Signup and view all the answers

<p>structure</p> Signup and view all the answers

<p>amino acids</p> Signup and view all the answers

<p>metabolic</p> Signup and view all the answers

<p>proteins</p> Signup and view all the answers

<p>identity</p> Signup and view all the answers

<p>metabolic</p> Signup and view all the answers

<p>enzymes</p> Signup and view all the answers

<p>proteins</p> Signup and view all the answers

<p>identity</p> Signup and view all the answers

<p>metabolic</p> Signup and view all the answers

<p>amino acids</p> Signup and view all the answers

<p>cysteine</p> Signup and view all the answers

<p>conformation</p> Signup and view all the answers

<p>enzymes</p> Signup and view all the answers

<p>amino acids</p> Signup and view all the answers

<p>sickle-shaped</p> Signup and view all the answers

<p>Denaturation</p> Signup and view all the answers

<p>substrates</p> Signup and view all the answers

<p>denatured</p> Signup and view all the answers

<p>beta</p> Signup and view all the answers

<p>polypeptide</p> Signup and view all the answers

<p>side chains</p> Signup and view all the answers

<p>basic</p> Signup and view all the answers

<p>hydrophobic</p> Signup and view all the answers

<p>proteins</p> Signup and view all the answers

<p>quaternary</p> Signup and view all the answers

<p>sheets</p> Signup and view all the answers

<p>function</p> Signup and view all the answers

<p>stabilized</p> Signup and view all the answers

<p>spiral</p> Signup and view all the answers

<p>structure</p> Signup and view all the answers