protein Insulin (also see Fig 14.24) Ferritin Myoglobin Hemoglobin Ribonuclease a-keratin Collagen Has intramolecular disulfide bond(s) Every third residue is a glycine Globular Fibrous protein Rich in protein a helices and B turns Rich in a helices only Has helical polypeptide chain (not a helices)
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Check off the characteristics that describe each protein structure.
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- Both a-keratin and collagen are fibrous proteins.however,the hydrogen bonding pattern is different between the helices of the respective proteins.what os the major difference?Which amino acid sequence will form part of which protein structure, and why? Sequence 1: Ser-Phe-Gln-Val-Lys-Leu-His-Tyr-Asp-Val Sequence 2: Glu-Tyr-Leu-Asn-Phe-Ala-Gln-Val-Leu-Arg __Amphipathic beta strand __ Amphipathic alpha helixcip sequence rule in ephedrine
- fexoting WA Auler Shape Ser Comert Seatwork CH2 CH - Identify the type of bond(s) that stabilizes the protein structures. H,C H,C CH, CH CH HO -C disaltide brnd hy dnphic interation Ismic bmd CH2 CH2 S-SCH, 2 CH, NH, -o-c-CH, 4NAZO NHZ Ala-Cys-Glu -Tyr - Trp - Lys - Arg - His -Pro-G ly Glu pka 4.15 SH Tyr 10.10 Draw Charges Lys 10.67 Olt A3 12.10 +NH₂ Ntrm 2) Calculate net charge 3) write out I letter code 300 Ctim 3 juli of peptich (above) Ⓒ pH; 1,7,12Thesecondarystructureofaproteinisinfluencedbybothhydrogen bonding and London dispersion forces. a. Usingastructuralformula,showanexampleofhydrogenbonding between the serine portion of a protein and the tyrosine portion b. Usingastructuralformula,showanexampleofLondondispersionforces between the leucine portion of a protein and the valine portion
- Hydropathy & Amphipathicity 2 -1 -2- 110 210 310 410 510 Residue Number C. Draw the topology of this membrane protein in the bilayer and indicate the range of residues forming transmembrane a-helices.Draw the structure of this peptide: N-Met-His-Tyr-Leu-Asp-Ser-Arg-Leu-CUpload a drawing of Gly-Met-Asn-Glu-His Label the alpha carbons Label the R groups as hydrophobic or hydrophilic Label the acidic and basic R-groups Label the peptide bonds Label the N terminus and the C terminus
- 1. Consider the following α helix from myoglobin at pH 7. Gln-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-His-Phe-Arg-Lys-Asp-Ile-Ala-Ala-Lys-Tyr(a) Label amino acids in the polypeptide above as follows: p for polar and uncharged, np for non polar, – for negatively charged, and + for positively charged.(b) How many complete turns are there in this helix?(b) Which side chains are likely to be on the side of the helix that faces the aqueous solvent? Why?(c) Which side chains are likely to face the interior of the protein? Why?Tt 7. What is the driving force that promotes secondary structure formation of alpha helices and beta sheets? How is this force arranged to make an alpha helix or beta sheet? What promotes turns or kinks in these structures? You can describe and/or draw it but please show what are the interactions facilitating this effect.Estimate the number of amino acid residues in each of the two helices of a segment of the alpha-keratin coiled coil that is 23 nm long.