Proteins have complex three-dimensional structures. These polymers are held into these specific shapes with a variety of intermolecular forces, covalent bonds, and ionic bonds. Alpha-helices and beta-sheets are examples of A) primary structure B) secondary structure C) tertiary structure D) quaternary structure
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- Which one of the following types of bond is principally responsible for holding the α-helix shape of a protein secondary structure : A) peptide B) disulfide C) hydrogen D)ionicUsing the appropriate chemical structures describe the monomers and polymers for each of the following macromolecules; a) fats b) nucleic acid2. Identify the structural level in each protein. A) quaternary structure B) tertiary structure C) secondary structure D) primary structure 1) The protein folds into a compact structure stabilized by interactions between R groups. 2) the combination of two or more protein molecules to form an active protein 3) B-pleated sheet 4) the peptide bonds betwecen the amino acids 5) the structural level achieved when hydrogen bonds form between the carboxyl group of one amino acid and the amino group of a different amino acid
- A coiled peptide chain held in place by hydrogen bonding between peptide bonds in the same chain is : A) Alpha helix B) Primary structure C) Tertiary structure E) Beta pleated sheetsThe most important contribution to the stability of a protein's conformation appears to be the: ○ A) entropy increase from the decrease in ordered water molecules forming a solvent shell around it O B) large entropy increase from ionic interactions between the ionized amino acids in a protein C) sum of the free energies of many weak interactions among the hundreds of amino acids in a protein ○ D) sum of free energies of formation of many weak interactions between polar amino acids and surrounding water E) stabilizing effect of hydrogen bonding between the carbonyl group of one peptide bond and the amino group of anotherPeptide bonds cannot rotate. This is because: a) the amino acid side chains are too bulky to allow this. B) Internal hydrogen bonding hinders rotation. C) interaction with water molecules hinders rotation D) the peptide bond has considerable double bond character Polypeptide chains prefer the trans conformation. This is because: a) This distances hydrophilic groups from hydrophobic groups b) this minimizes crowding of side chains c) This brings hydrophilic groups in contact with water molecules d) This allows proteins to fold more easily Ramachandran plots indicate that protein conformation is largely a function of: a) hydrophobicity b) number of amino acids c) torsion angles d) arrangement of prosthetic groups
- The tertiary structure of a protein is the : A) overall protein structure resulting from the aggregation of two or more polypeptide subunits. B) order in which amino acids are joined in a polypeptide chain. C) bonding together of several polypeptide chains by weak bonds. D)organization of a polypeptide chain into an α helix or β pleated sheet. E)unique three-dimensional shape of the fully folded polypeptide.7. Native conformation of proteins may result from: a) hydrophobic interactions b) H-bonds c) ionic bonds d) covalent bonds e) all a-d may contribute to native conformationWhich of the following statements is true about the quaternary structure of a protein? A) The quaternary structure of a protein is based on how polypeptide subunits interact with one another. B) The quaternary structure of a protein is affected by hydrogen bonds. C) The quaternary structure is the overall shape of a protein. D) The quaternary structure is driven by a- helices and B-pleated sheets. E) The quaternary structure is found in all proteins.
- The protein pictured has .. O A) primary structure B) secondary structure C) tertiary structure D) quaternary structure E) all of the aboveProper 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 structureIn Protein structure: a). Write the name of the four levels of protein structure, b). Explain the structural characteristics at each level,