Course Structure Quiz

<p>Evolution of plant functions (A)</p> Signup and view all the answers

<p>20% (B)</p> Signup and view all the answers

<p>Depend on technical issues as valid excuses (A)</p> Signup and view all the answers

<p>October 14 to 18 (D)</p> Signup and view all the answers

<p>Convergent/divergent evolution of domains (C)</p> Signup and view all the answers

<p>It initiates bacterial polypeptide translation. (C)</p> Signup and view all the answers

<p>Eukaryotic mRNA is monocistronic and codes for a single protein. (C)</p> Signup and view all the answers

<p>The AUG initiation codon (A)</p> Signup and view all the answers

<p>The physical structure and function of each enzyme. (C)</p> Signup and view all the answers

<p>To recognize stop codons. (A)</p> Signup and view all the answers

<p>They reinforce the secondary structure. (A)</p> Signup and view all the answers

<p>The linking of amino acids to tRNA by aminoacyl-tRNA synthetase. (B)</p> Signup and view all the answers

<p>20 unique enzymes, one for each amino acid. (C)</p> Signup and view all the answers

<p>They have a unique structure that corresponds to each amino acid. (A)</p> Signup and view all the answers

<p>It binds to a specific amino acid through an acyl linkage. (D)</p> Signup and view all the answers

<p>Class I aminoacyl-tRNA synthetase. (B)</p> Signup and view all the answers

<p>Approximately 80%. (C)</p> Signup and view all the answers

<p>It is ready to accept an amino acid. (B)</p> Signup and view all the answers

<p>Phe, His, Thr (B)</p> Signup and view all the answers

<p>Metabolic fuels (C)</p> Signup and view all the answers

<p>DNA makes RNA, which makes proteins (D)</p> Signup and view all the answers

<p>Amino-acid chain (C)</p> Signup and view all the answers

<p>Alanine (B)</p> Signup and view all the answers

<p>Membrane stabilization (D)</p> Signup and view all the answers

<p>Carry amino acids to ribosomes (C)</p> Signup and view all the answers

<p>Glycine (C)</p> Signup and view all the answers

<p>To increase the rate of chemical reactions (A)</p> Signup and view all the answers

<p>Collagen (D)</p> Signup and view all the answers

<p>Fibrous proteins appear in body structures. (D)</p> Signup and view all the answers

<p>An amino acid with both a basic amino group and an acidic carboxyl group (B)</p> Signup and view all the answers

<p>Histidine can act as both an acid and a base around pH 6.04. (D)</p> Signup and view all the answers

<p>To provide structural support and enable cell motility (D)</p> Signup and view all the answers

<p>They primarily include enzymes and antibodies. (B)</p> Signup and view all the answers

<p>Functional proteins include enzymes and catalyze reactions. (C)</p> Signup and view all the answers

<p>The acid dissociates protons more readily. (C)</p> Signup and view all the answers

<p>The pH at which protonated and deprotonated forms are in equal amounts. (D)</p> Signup and view all the answers

<p>pH 7.04 (B)</p> Signup and view all the answers

<p>It becomes positively charged. (D)</p> Signup and view all the answers

<p>The pH at which the amino acid has no net charge. (C)</p> Signup and view all the answers

<p>It alters the balance between protonated and deprotonated forms. (C)</p> Signup and view all the answers

<p>Both forward and reverse reactions occur simultaneously. (C)</p> Signup and view all the answers

<p>The acid will be mostly deprotonated. (A)</p> Signup and view all the answers

A core concept in the course focusing on the relationship between protein shapes and their roles.

Course code for Protein Structure and Function.

Breakdown of components in assessing student performance in the course.

November 5th is the last date to withdraw from the course without academic penalty.

The midterm exam is scheduled for October 29th.

A plan outlining the lecture timing and important examination dates.

Composition, chemistry, structure & function, and application of proteins in research.How structure relates to function, proteomic info, how proteins function and evolve.

Rules, procedures, and expectations for student conduct in the course.

Proteins perform diverse roles in organisms, acting as structural components, catalysts, antibodies, and regulators.

Biological catalysts that speed up chemical reactions in living organisms.

Enzymes are crucial for biological processes; without them, essential metabolic reactions would be too slow for life.

Proteins that form the structural components of organisms, like collagen and keratin.

A protein that polymerizes to make filaments, essential for cell movement and contraction.

Proteins that have a roughly spherical shape and usually function in metabolic processes, such as antibodies and enzymes.

A molecule with both positive and negative charges, but a net charge of zero, found in amino acids at a specific pH.

Basic building block of proteins, having an amino group, a carboxyl group, and a unique side chain (R group).

A polypurine sequence in bacterial mRNA, located around 10 bases upstream of the AUG start codon, that helps recruit the ribosome for translation initiation.

A type of mRNA that encodes for multiple proteins, often found in bacteria, where one mRNA transcript can be translated into several different polypeptide chains.

A type of mRNA that encodes for a single protein, commonly found in eukaryotes, where each mRNA transcript directs the synthesis of only one polypeptide chain.

A continuous stretch of DNA or RNA that starts with a start codon (usually AUG) and ends with a stop codon, defining the region that encodes for a specific protein.

The rate at which ribosomes translate mRNA into protein, measuring the number of amino acids added per second.

A measure of acid strength in solution. The higher the Ka value, the stronger the acid.

The pH at which a molecule has an equal amount of protonated and deprotonated forms.

The pKa of the histidine side chain is ~6.04. This means at pH 6.04, histidine exists in a 50/50 mixture of protonated and deprotonated forms.

At pH below 6.04, most histidine residues are protonated (+1 charge). At pH above 6.04, most histidine residues are deprotonated (neutral).

The pH at which a molecule has a neutral overall charge.

The pI of a protein is determined by the average pKa of all its constituent amino acids.

At its pI, a protein has no net charge and will not migrate in an electric field.

The pI of a protein is important for its solubility, stability, and interactions with other molecules.

The local 3D structure of a polypeptide chain, formed by hydrogen bonds between backbone atoms. Examples include alpha-helices and beta-sheets.

A secondary structure in proteins characterized by a right-handed helical structure stabilized by hydrogen bonds between backbone atoms.

A secondary structure in proteins consisting of extended polypeptide chains arranged side by side, held together by hydrogen bonds between backbone atoms.

Transfer RNA (tRNA) has a unique 3D structure crucial for its function in protein synthesis. It folds into a cloverleaf-like shape with distinct loops and arms.

The process of attaching an amino acid to its corresponding tRNA molecule. This is catalyzed by aminoacyl-tRNA synthetases, which recognize both the tRNA and the amino acid.

Enzymes that catalyze the attachment of a specific amino acid to its corresponding tRNA molecule, ensuring accuracy and efficiency in protein synthesis.

Two classes of aminoacyl-tRNA synthetases exist: Class I interacts with tRNA at the minor groove, and Class II interacts with tRNA at the major groove. This difference in interaction allows for specific recognition and attachment of the correct amino acid.

A set of rules that dictates the correspondence between codons in mRNA and amino acids in proteins. There are 64 codons, but only 20 amino acids, resulting in degeneracy where multiple codons can code for the same amino acid.

Amino acids that the body cannot synthesize and must be obtained from the diet.

Amino acids that the body can synthesize from other molecules.

The process of converting amino acids into other molecules, such as glucose, fatty acids, or ketone bodies.

The fundamental principle that describes the flow of genetic information from DNA to RNA to protein.

tRNA molecules transport specific amino acids to ribosomes during protein synthesis. Aminoacyl-tRNA synthetases link amino acids to their corresponding tRNAs.

The cellular machinery responsible for protein synthesis, composed of rRNA and proteins.

The unique sequence of amino acids in a polypeptide chain, determined by the genetic code.