How many amino acids are present on the helix to the right? Any partially drawn amino acids count as one whole amino acid Circle one peptide bond and box one R group on the figure to the right Describe how a lack of Vitamin C in the diet will affect the overall structure of collagen.
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- "The elasticity of elastin derives from its high content of a helices, which act as molecular springs" is true or false.For the protein given in the attached picture: Write the name of these 5 amino acids corresponding to their abbreviation of 3 letters. Describe precisely how the functional groups in the amino acids are involved in bonding between two successive amino acids in the protein.Label: 1) the type of chemical bonds between the amino acids (e.g. covalent bond, ionic bond, metallic bond) 2) the type of interparticle forces of attraction occurring within the protein and with its environment *Indicate at least four observed interparticle forces of attraction *pink - negatively charged, blue - positively charged, yellow - nonpolar and uncharged, green - polar and uncharged *[See example picture] The chemical bond (shown by the arrow) is depicted as a line between the amino acids. Interparticle forces of attraction, such as the one between Phe and Glu (boxed), are not represented by lines but rather by the proximity of amino acids.
- After the peptide chain of collagen has been formed, many of the proline residues are hydroxylated on one of the ring carbon atoms. Why is this process important for the triple helix of collagen?Amino acids are the building blocks for proteins in the cell. The structures of the amino acids glutamate (or glutamic acid), glycine, and leucine are provided below in the same order from left to right. Map any chiral centers with a 1.1.Leucine is shown below. Suppose this amino acid was used to form the protein sequence Arg-Phe-Leu-Met-Pro. Select any atom that will be part of the protein backbone 2.This cartoon pf the protein hormone insulin illustrates what spaces of insulins structure? primary structure secondary structure tertiary structure quaternary structure
- At what level of protein structure (primary, secondary, tertiary, or quaternary) will protein structure be initially altered? Heating a protein (due to fever), causing hydrogen bonds to break. Drastic changes in pH (like the above patients), causing some polar amino acids to turn into non-polar amino acidsThe term protein is generally used for polypeptide with 40 or greater amino acid residues 100 or greater amino acid residues 20 or greater amino acid residues 500 or greater amino acid residuesAmino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
- Collagen is composed of the collagen triple helix containing 1042 amino acids, How long is the collagen triple helix in Angstroms?If you were given the abbreviations for 4-6 amino acids, could you draw the polypeptide chain AND determine its isoelectric point? Do this for the amino acid Asp-Arg-Val-Tyr-IleWrite the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU I NEED IT ASAP PLEASE
