A small generic section of the primary structure of an a helix is given by -amino acid, -amino acid,-amino acid,-amino acid,-amino acid,-amino acid,-amino acid,– Which amino acid residue's backbone forms a hydrogen bond with the backbone of the seventh (7th) residue?
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- Describe the amino acid illustrated above (at pH = 7.0). (the following amino acid at pH = 7 (aqueous form): (COO-)–CH(NH3+)–CH2–(COO-)) it is a non-polar, positively-charged amino acid it is a polar, positively-charged amino acid it is a polar, uncharged amino acid it is a polar, negatively-charged amino acid it is a non-polar, negatively-charged amino acidWhich amino acid residue's backbone forms a hydrogen bond with the backbone of the fifth (5th) residue? Which peptide segment is most likely to be part of a stable a helix at physiological pH? -Tyr-Trp-Phe-Val-Ile- -Glu-Leu-Ala-Lys-Phe- -Gly-Gly-Gly-Ala–Gly- -Gly-Arg-Lys-His-Gly- -Pro-Leu-Thr-Pro–Trp- -Lys-Lys-Ala-Arg-Ser- -Glu-Glu-Glu–Glu–Glu, MacBook ProDescribe the amino acid illustrated here (Identify the following amino acid (at pH = 7.0): (COO-)–CH(NH3+)–CH2–CH2–CH2–CH2–(NH3+)) (at pH = 7.0). it is a polar, negatively-charged amino acid it is a non-polar, negatively-charged amino acid it is a polar, positively-charged amino acid it is a non-polar, positively-charged amino acid it is a non-polar, uncharged amino acid
- Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?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)β-pleated sheets and α-helices arise more from interactions in the peptide backbone than from the “R” groups of the individual monomers; they are examples of the (????) structure of a protein. Primary Tertiary Secondary Quaternary (????) are comprised of a nitrogenous base, a pentose sugar, and a phosphate group. Monosaccharides Amino acids Proteins Nucleotides (????) is the RNA transcript of the DNA sequence that determines the primary structure of a protein. mRNA lncRNA tRNA rRNA If a substance such as a lipid isn’t soluble in water it might be described as (????) Hydrophilic Hydrophobic
- Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a positively charged amine group? (Choose one answer) the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structureWhich of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (8) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (€) They require a high content of proline and glycineThe structure of an alpha helix orients the oxygens of the carbonyl group of the peptide bond towards the C-terminal end of the helix while the hydrogens of the NH groups orient toward the N-terminal end, thus imparting a dipole along the length of the helix. As a result, which kinds of amino acids would favor the C-terminal end, and which would favor the N-terminal end? negatively charged, positively charged positively charged, negatively charged negatively charged, hydrophobic positively charged, hydrophobic hydrophobic, negatively charged hydrophobic, positively charged
- Which of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (B) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (E) They require a high content of proline and glycineA 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).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