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protein struture/fun
| Question | Answer |
|---|---|
| Select all of the following that make up the components of an amino acid: | amino group carboxyl group variable side chain |
| The covalent bond between amino acid in a polypeptide chain is called a _____ bond. | peptide |
| Which of the following non-covalent interactions are involved in the folding of the 3D structure of proteins (select all that apply): | hydrogen bonds electrostatic attractions van der Waals attractions hydrophobic forces |
| Protein secondary structure primarily results from _____ bonds. | hydrogen |
| The complete three-dimensional structure of a fully folded protein is its _____ structure. | tertiary |
| A protein whose quaternary structure consists of two identical, folded polypeptide chains is called a _____. | dimer |
| Proteins that help fold proteins into their correct conformation are called _____ proteins. | chaperone |
| Many neurological disease are associated with incorrectly folded proteins that aggregate into clumps called amyloid structures that are stabilized by the stacking of _____. | b sheets |
| Any segment of a polypeptide chain that can fold independently into a compact, stable structure is called a(n) _____. | domain |
| An important function of proteins is transport. How are globin proteins able to sense and transport oxygen? | by use of the heme cofactor to reversibly bind oxygen to an iron atom |
| How does adding or removing phosphates affect protein function? | by changing the shape which alters the function |
| Proteins can be modified by covalent modifications. What does the addition of a covalently attached ubiquitin molecule signal? | destruction of the protein |
| What does tertiary protein structure refer to? | The full 3D conformation of a single polypeptide chain |
| In aqueous conditions, where are hydrophobic amino acids typically located in a folded globular protein? | Inside the folded protein |
| What does quaternary protein structure involve? | The arrangement of multiple polypeptide chains |
| What is the function of chaperone proteins? | They assist in protein folding and prevent aggregation |
| What is DnaK (Hsp70) in bacteria? | A chaperone protein that assists in protein folding |
| What is the function of GroEL/ES (Hsp60/Hsp10) in bacteria? | It provides a cage-like compartment for protein folding |
| What factors determine protein specificity for binding to other molecules? | Affinity (chemistry) and selectivity (conformation) due to non-covalent interactions |
| What is lysozyme? | An enzyme that breaks down bacterial cell walls |
| Which enantiomer of amino acids is typically found in proteins? | L-enantiomers |
| How much faster can enzymes make reactions occur compared to uncatalyzed reactions? | A million times faster (or more) |
| What is a cofactor? | An ion, molecule, or compound required for enzyme function |
| What is the function of protein kinases? | They add phosphate groups to proteins (usually to serine, threonine, or tyrosine) |
| What is the function of ubiquitin as a covalent modification? | It tags proteins for destruction |
| What is negative feedback in protein regulation? | High product levels lead to the process being slowed or stopped |
| What is allosteric regulation? | Regulation where a molecule binds to a site other than the active site, causing a conformational change |
| What is the function of scaffold proteins? | They link specific sets of proteins at specific sites, promoting rapid collisions |
| How many standard amino acids are in the genetic code? | 20 |
| Which two non-standard amino acids are naturally incorporated into proteins by using different readings of stop codons? | Selenocysteine and Pyrrolysine |
| What type of bonds primarily stabilize secondary protein structure? | Hydrogen bonds |
| What is an example of a protein with beta (pleated) sheet structure? | Fibroin (found in silk) |
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