Biological Functions of Proteins

Microtubules and collagen are two structural components formed by proteins.

Enzymes primarily function as catalysts in various cellular reactions.

Proteins, such as plasma proteins and hemoglobin, aid in the transportation of various molecules.

<p>Amino acids have a central carbon atom, a carboxyl group, an amino group, and a side chain.</p> Signup and view all the answers

<p>Proline is unique because it contains a secondary amino group in its structure.</p> Signup and view all the answers

<p>Protein conformation is crucial because it determines the protein's specific biological functions.</p> Signup and view all the answers

<p>Motor molecules, such as actin and myosin, are involved in carrying membrane-enclosed organelles.</p> Signup and view all the answers

<p>The 20 standard amino acids and their unique side chains enable the formation of a diverse array of proteins.</p> Signup and view all the answers

<p>The main driving forces are non-covalent interactions such as hydrogen bonds, electrostatic interactions, and hydrophobic interactions.</p> Signup and view all the answers

<p>Hydrophobic interactions help stabilize the three-dimensional arrangement of proteins by minimizing exposure of hydrophobic side chains to the aqueous environment.</p> Signup and view all the answers

<p>Fibrous proteins are arranged in long strands or sheets, while globular proteins are folded into a spherical or globular shape.</p> Signup and view all the answers

<p>The amino acid sequence determines how the protein folds, which directly influences its overall shape and function.</p> Signup and view all the answers

<p>Protein stability refers to the tendency to maintain a native conformation, which is crucial for the protein's proper function and the cell's survival.</p> Signup and view all the answers

<p>The quaternary structure is characterized by the interaction of two or more folded polypeptide chains.</p> Signup and view all the answers

<p>Alterations in protein shape can reduce or eliminate protein function, potentially disrupting cellular processes necessary for survival.</p> Signup and view all the answers

<p>Secondary structures, such as alpha helices and beta sheets, provide foundational shapes that contribute to the overall three-dimensional arrangement in tertiary folding.</p> Signup and view all the answers

<p>Hydrophobic interactions primarily drive protein stability by preferentially burying hydrophobic groups away from water.</p> Signup and view all the answers

<p>The contribution of the hydrophobic effect generally varies proportionately with size, always making a contribution greater than 50%.</p> Signup and view all the answers

<p>Hydrogen bonds contribute significantly to protein stability, ranking just below hydrophobic interactions in importance.</p> Signup and view all the answers

<p>Hydrophobic interactions and hydrogen bond interactions are two key types involved in protein stabilization.</p> Signup and view all the answers

<p>Environmental stress conditions like improper pH or high temperature can lead to protein unfolding.</p> Signup and view all the answers

<p>Van der Waals interactions are non-covalent forces that play an important role in maintaining protein stability.</p> Signup and view all the answers

<p>Electrostatic interactions influence stability and functionality through the formation of salt bridges.</p> Signup and view all the answers

<p>The burial of hydrophobic and uncharged polar groups implies increased complexity in protein interactions and stability.</p> Signup and view all the answers

<p>m-RNA reads the genetic information encoded in DNA and directs the synthesis of proteins by conveying this information to t-RNA.</p> Signup and view all the answers

<p>Modified amino acids have additional chemical groups or structures which can alter their properties and functions compared to standard amino acids.</p> Signup and view all the answers

<p>The primary structure determines the unique sequence of amino acids in a protein, which is crucial for its overall conformation and activity.</p> Signup and view all the answers

<p>The secondary structure refers to local folding patterns within the polypeptide backbone, typically forming structures like helices and pleated sheets.</p> Signup and view all the answers

<p>Glucogenic amino acids can be converted into glucose, while ketogenic amino acids can be converted into ketone bodies.</p> Signup and view all the answers

<p>t-RNA transports specific amino acids to the ribosome, matching them to the corresponding codons on the m-RNA during translation.</p> Signup and view all the answers

<p>Non-ribosomal peptide synthase facilitates the synthesis of certain peptides that are not assembled via ribosomal mechanisms, using monomers like homoalanine.</p> Signup and view all the answers

<p>The amino acid sequence dictates the protein's folding patterns and its resulting structure, which directly influences its function and catalytic activity.</p> Signup and view all the answers