Which statement about intrinsically disordered proteins is true? ○ They contain small hydrophobic cores ○ They represent misfolded conformations of cellular proteins ○ Lack of stable three-dimensional structure precludes a role in cellular function ○ They are responsible for proteostasis ○ They can be central players in protein interaction networks
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- Proteins are synthesized by a reaction called__________synthesis, which releases______________ . Subunits of proteins are called________ . The sequence of protein subunits is called the_________ structure of the protein. Two regular configurations of secondary protein structure are__________ and________ . When a protein’s secondary or higher-order structure is destroyed, the protein is said to be__________ .What level of protein structure is least likely to be affected if a protein's environment experiences a shift in pH below its optimal range? A. Quaternary B. Secondary C. Primary D. TertiaryWhich levels of protein structure are determined by primary structure mark all that apply 1. secondary structure (alpha helices and/or beta sheets) 2. tertiary structure (the folded, three-dimensional shape of a protein) 3. amino acids 4. peptide bonds
- Which of the following, if any, is correct about protein folding? a)2° structure formation is primarily entropic, 3° structure formation is primarily entropic b)2° structure formation is primarily entropic, 3° structure formation is primarily enthalpic c)2° structure formation is primarily enthalpic, 3° structure formation is primarily entropic d)2° structure formation is primarily enthalpic, 3° structure formation is primarily enthalpic e)None of the aboveProteins are the dominant structural and functional molecules in a cell. Which one of the following statements about proteins is NOT correct? A. The native conformation of a protein is usually arrived at very quickly after synthesis. B. Hydrogen bonding is the only type of bonding that gives rise to secondary structure. C. Urea denatures proteins by disrupting the interactions among non-polar (hydrophobic) amino acids D. Most proteins consist of a single polypeptide and thus do not have quaternary structure.Which levels of protein structure are determined by primary structure (i.e. the specific amino acid sequence beginning at the amino terminus of the polypeptide)? Mark all that apply. 1. secondary structure (alpha helices and/or beta sheets) 2. tertiary structure (the folded, three-dimensional shape of a protein) 3. amino acids 4. peptide bonds
- Proper folding is essential for most proteins to function. Which of the following statement about protein folding are correct. There may be more than 1 right answer. a) changing the primary sequence will change the final conformation b) desaturation results in a protein that has a higher free energy than the native conformation c) protein spontaneously fold into their correct shape d) denatrutation will cause a protein to lose its tertiary structureWhich of the following describes a primary protein structure?A) Protein structure maintained by disulfide linkages.B) Amino acid sequence maintained by peptide bonds.C) Protein chains maintained by interactions of peptide backbones like an α-helix.D) Arrangement of multiple protein subunits.E) Protein structure maintained through multiple hydrogen bonds.Protein structures have several different levels of organization. In the space below indicate the type of molecular bonds that can contribute to each level of organization: primary- secondary- tertiary- quarternary-
- At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? Heating a protein (due to fever), causing hydrogen bonds to break. Drastic changes in pH (like the above patients), causing some polar amino acids to turn into non-polar amino acidsWhat level of protein structure includes polypeptide aggregates? A. Secondary B. Quaternary C. Primary D. TertiaryWhich of the following types of molecular interactions play a role in protein folding? Select all that apply. A. Covalent bonds B. Hydrogen bonds C. Van der Waals attraction D. Hydrophobic interactions