Which is responsible for the stabilization of parallel polypeptide chains in a beta-pleated sheet conformation? O Van der Waals covalent bonding R-group interactions H-bonding
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- Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.The synthetic process by which monomers are covalently linked is (a) hydrolysis (b) isomerization (c) condensation (d) glycosidic linkage (e) ester linkageWhich of the following factors do not stabilize the 3-D structure of a folded protein? O Disulfide bonds O Van der Waals interactions O Hydrogen bonds O Electrostatic interactions O Hydrophobic bonds Metal-ion protein interactions
- Choose the best response for each of the blanks in the statement below. When it is part of a polypeptide chain, proline is a known disruptor of [Select] because of [Select] [ Select ] its hydrophobic character the strain brought about by the five-membered ring the lack of an amino hydrogen in the backbone the lack of a freely moving side chain Select ] primary structure secondary structure tertiary structure quaternary structureWhat types of interactions are possible between the side chains of the polypeptide shown below? Select all that apply: *NH, он SH SH H H N, N, N, H H H NH2 *NH, O Disulfide bonds O Hydrogen bonds lonic bonds O Hydrophobic interactionsThe dihedral or torsion angles of polypeptide backbone, the allowed values of which are summarized by the Ramachandran diagram, refer to rotation of the following pair of bonds. Cα-N and Cα-R C=O and Cα-N C-N and Cα-C Cα-C and Cα-N Cα-R and Cα-C
- In α-helices - what is the length of the hydrogen bonds between: TYR41H and GLU37O ALA39H and MET35O GLU38H and ILE34O THR36H and ARG32O. ARG32H and TYR28OThe different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bondsGiven the polypeptide chain below: Alanine - Arginine - Valine - Histidine - Aspartic acid - Glutamic acid Ala-Arg-Val-His-Asp-Gln How many peptide bonds are there? What kind of polypeptide is it?
- A peptide has the sequence: glu-trp-ser-gly-leu-lys-pro-gly What is the net charge of the molecule at pH 3,8,11 (only two side chain are ionizable).Draw a polypeptide chain with the following sequence of amino acids: M-A-N-A-N-D-G-E-N-EThe R-group of lysine has an overall positive charge. The R-group of glutamic acid has an overall negative charge. Within the structure of a protein molecule, these two amino acids will: O attract each other O repel each other O form a disulfide bridge O form a pure covalent bond
