Tertiary structures refer to the three-dimensional arrangement of every atom in the molecule. On the other hand, primary structures refer to the stable arrangements of amino acid residues in a protein that give rise to recurring patterns. Both statements are correct O Both statements are incorrect O The first statement is incorrect while the second statement is correct The first statement is correct while the second statement is incorrect
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- it is widely accepted that proteins can organize themselves according to a range of stable structural motifs. How is this knowledge exploited in the organization of the protein data blank?Which of the following levels of protein architecture is least likely affected by changes in pH? O Secondary Structure Quaternary Structure O Tertiary Structure O Primary Structureion 65 A group of biologists developed a drug that target a specific protein and inhibit its function. This drug cuts the bonds between strongly positive and strongly negative sides of the protein. Which level of protein structure would be affected directly by this drug? et ered ed out of Select one: uonsənb 61 O a. Quaternary structure O b. Secondary structure Oc. Tertiary structure O d. Primary structure e. B pleated sheet
- Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data Consider the following amino acid sequence Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg Where might reverse turns occur? Where might Intrachain disulfide linkages be formed? What will be the secondary structure formed from this sequence? Assuming that this sequence is part of a larger globular protein, indicate the probable location of the following amino acid residues: Asp, Ile, Thr, Ala. Gln, Lys.( Hint: see Hydropathy index)Show below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys CysPart A What is the highest structural level of protein structure represented in the following image? primary quaternary secondary pentanary tertiary O O
- Which of the following statements about protein structure is CORRECT O a. Fibrous proteins can have rigid quaternary structure O b. The stability of the quaternary structure in proteins is mainly a result of covalent bonds among the subunits O c. The denaturation of proteins always leads to irreversible loss of secondary and tertiary structure d. The information required for the correct folding of a protein is contained in the specific sequence of amino acids along the polypeptide chain O e. The formation of a disulfide bond in a protein requires that the two participating cysteine residues be adjacent to each other in the primary sequence of the proteinA protein has a mutation of a glycine to a lysine. Which best predicts the impact of this mutation on the overall protein structure and function? H.N, *NH3 Glycine Lysine O A small hydrophobic amino acid has been replaced with a large hydrophilic amino acid, and this may change folding O A small hydrophilic amino acid has been replaced with a large hydrophobic amino acid, and this may change folding O These residues are similar in chemical properties, and there will be little impact on folding O This mutation may disrupt hydrogen bonds, which would disrupt the tertiary structureIf a protein that contains one peptide chain has no cysteine residues, which step(s) in the chemical strategy for determining primary structure is NOT required? O Cleavage of intrachain disulfide bonds O Alternate fragmentation and sequencing to generate overlapping sequences O Construction of the overall protein sequence O Terminal residue identification O Separation and purification of peptide chains O Peptide chain fragmentation and sequence determination O Pinpointing the location of disulfide bonds
- The primary structure of proteins results from (choose the best answer) O assistance from chaperonin enzymes O the sequence of amino acid subunits that make up the protein polymer O the twisting, bending, and coiling resulting from hydrogen bonds into spirals and sheets O the folding and reshaping that results from hydrophobic interactions and the formation of disulfide bridges between cysteine amino acids in the polymerOftentimes, the major challenge in the determination of protein structure via X-ray crystallography is the production of good crystals. One common approach is to crystallize fragments of the whole protein instead of crystallizing the whole protein. If you were to cleave a protein into fragments that will still retain the folding of that fragment in the whole protein, where is the best location to perform the cleavage? O At the ends of each alpha helix. O At the ends of a protein motif. O At the points connecting protein domains. O At the ends of beta strands.Give 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