using the expanded structure of Levothyroxine. Determine the molecular geometry of each central atom.
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using the expanded structure of Levothyroxine.
- Determine the molecular geometry of each central atom.
Color each central atom based on its molecular geometry and include a key for your colors. For example, color tetrahedral C’s red, trigonal planar C’s , blue, etc.
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- Gentiobiose (D-Glc(ß1→6)D-Glc) is a disaccharide found in some plant glycosides. Draw the Haworth structure of gentiobiose based on its abbreviated name. Show all multiatom groups using the groups tool. Show stereochemistry using wedge (upward) or dash (downward) bonds.Describe the important biochemical properties of carbohydrates and why carbohydrates would be considered polar molecules. A▾ B I X @ F 7Differences between Cis-fatty acid VS. Trans fatty acids Limit your answer to two sentences only to every question. Copy and complete the table. GIVEN: DRAW THE EXPANDED STRUCTURE NAME THE BONDS [Molecular Orbitals &Hybrid Orbitals] IUPAC NAME CHOOSE THE SIMPLEST Unsaturated FATTY ACID NAME OF THE COMPOUND Cis-fatty acid Trans-fatty acid
- Given the following choices,a. structure of sterolb. what is the structure of a glycolipid?Modify isoleucine to show the predominant forms at pH 1, 7, and 13. Isoleucine has p?ap�a values of 2.4 (carboxyl group) and 9.7 (amino group).I. Write a balanced chemical reaction, complete with chemical structures, to show the hydrolysis of iso-C to U. II. Draw the mechanism by which iso-G converts to its "minor tautomeric form complementary to U." You may propose either an acid or base catalyst. III. Draw chemical structures of the minor tautomeric form of iso-guanine (iso-G) and uracil (U), showing the non-covalent bonding (H-bonding) interactions between them.
- Instructions: Write the structure of the following peptides in a bond paper and upload as pdf file . Expanded structure. Use red ink for peptide bond. [For your reference download all the amino acids with the three and single letter symbol] 1.) glycyl leucyl alanine 2.) tyrosyl alanyl glycine 3.) phenylalanyl tyrosyl seryl histidineConsider Isoleucine, structures are provided for the 4 stereoisomers, complete the table by assessing the R/S Configuration and assign appropriate Amino Acid name, choices are: L-Isoleucine, L-Allo Isoleucine, D-Isoleucine, D-Allo IsoleucineDescription Please draw the structure of the 19 L-a-amino acids and proline in any form, as you prefer. You may want to use a letter-size sheet or larger, it's up to you. Guiding principle: You want to understand the differences among amino acids. Although you may want to only draw the R-group it's preferable to draw it along with the rest of the molecule (i.e., the Ca, the amino group and the carboxyl group). Here are some examples (your drawings should not limited to the following styles): H₂C NH₂ OH shutterstock.com-222977980 Alanine H H Proline OH %%% lysine a alamy stock photo Tryptophan HN NH₂ shutterstock.com-1819000134 QH COOH H₂N-C- H CH ₂ Phenylalanine H₂N NH dreamstime.com arginine NH₂ OH
- Give at least 10 examples of biological compounds having an alkyne functional group and identify the biochemical importance of each compound.Analyze the following biomolecule using the criteria listed below. Be sure to be clear, concise, and complete with your responses. 1. What class of biomolecules does this compound belong to? Explain why. 2. Break this compound down into its components and clearly identify each section of the molecule by labelling (circle or draw an arrow to) its backbone structure, all functional groups, and all biomolecules in the structure. 00-P-O NH3 HOthe resonance stabilization of the amide linkage has profound effects on protein structure. Which of the following are the direct effect(s) of this on protein structure? Select all that apply All six atoms around the bond (including the Co) lie on the same plane There is no free rotation about the peptide bond. The bond between the carbon and the nitrogen in the peptide bond keeps "flickering" between being a single bond and a double bond. The peptide bond is polar. The nitrogen in the peptide bond cannot accept a hydrogen bond.