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- The 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 bondsThe following protein crystal structure is the Human Serum Albumin complexed with octadecanoic acid (PDB ID: 1E7I). According to the protein data bank, Human Serum Albumin is composed of 72% helical structure. Among the following options (a-c), select the possible Ramachandran plot for the above Human Serum Albumin. (a) (b) (c) Phi Phi PhiGive the force of interaction involved in the protein folding of the protein structure A and C: COO CH,C-N-H• • •0- Pleated sheet structure A H C Helical structure CH3 CH3 - CH3 -CHCH,CH, CH- CH, CH3 (CH,),NH, -0-CCH,- C=0..•HN CH, CH, CH,CH CH,CH CH, CH, CH OH 0=C -CH,-S,S-CH,- H,Ñ Structure A: H-bonding: Structure C: Van der Waals O Structure A: Covalent interaction; Structure C: dipole-dipole interaction O Structure A: Salt bridge: Structure C: H-bonding Structure A: Hydrophobic interaction; Structure C: ionic interaction 00000 B
- Amino acid structure and composition: Assuming physiological pH conditions, draw the peptide backbone of a protein composed of four amino acids. The protein is a) overall positively charged b) capable of forming disulfide bond with another protein c) has two amino acid that can participate in hydrogen bond formation d) one peptide bond in cis conformation you must show the complete name, single letter abbreviation and structure of each amino acid. Make sure to highlight the peptide bond that is in cis conformationWhat are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved. The molecule considered is a protein: pancreatic amylase.What are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved.
- Which type of motifs/folds are found in the protein shown below Coiled-coil O EF Hand O Horseshoe O Rossmann O Jelly roll O Greek key O Alpha/beta barrel O Beta barrel O Beta sandwich OZinc fingerMatch the protein structure terms on the left with the descriptions on the right. v (Choose ) commonly observed combinations of secondary structural elements tertiary structure Long segments of secondary structure. supersecondary structure basic component of quaternary structure Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptide Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chain compact structural or functional regions within a given polypeptide functional structures formed by non-covalent interactions between multiple polypeptides. domain (Choosel subunit quaternary structure (Choose)a. Suppose that the R group of a histidine residue in a protein in its native tertiary structure is buried in the interior of the protein and is involved in a salt bridge (ionic interaction) with an oppositely charged residue. Unfolding the protein exposes both of the charged groups to water. Would you expect the pKa of the His R group (side chain) in the native protein to be a) higher or b) lower than the pKa of the same residue in the unfolded protein? Why? b. Is the exocyclic NH2 in cytosine acidic or basic? Why? NH, `N'
- * Draw the tripeptide FTQ, making sure to care for stereochemistry.* Identify the N-terminus and the C-terminus of the peptide.* Identify what type of stabilizing interactions the amino acid side chains could employ in the tertiary andquaternary structure of a protein.in determining the structure of a fully folded protein? involving the amino acid side chains of the polypeptide. Which has the largest effect 5. hydrogen bonding ionic interactions a) b) c) d) hydrophobic interactions van der Waals interactions none of the above The misfolded, insoluble, and aggregated proteins characteristic of Alzheimer's disease and Parkinson's disease are known as: zymogens b) c) d) e) open quaternary structure proteins protein domains amyloid deposits molecular chaperones 6.Tt O 8. What are the driving forces that promotes tertiary -3D and quaternary -4D structure formation of proteins. Provide specific examples of the interactions that drive the formation of 3D and 4D structures?