Hi can someone help me please. The picture contains the full structure.

Please don't provide handwritten solution ....

Give correct detailed Solution with explanation needed of all options..don't give Handwritten answer

Only qno3m I think protein drawing has to show the bond interactions Onlyqno3 solve. I. Given a polypeptide below, answer the following questions: MAGGMIVIIGGMGCNSMVVVIIIGTSSCVIMEMMMIVKII Questions: 1. Enumerate all non-polar amino acids. (Provide the single letter and common name) 2. Enumerate polar amino acids include the acidic and basic types. (Provide the single letter and common name) 3. Illustrate the overall shape of the given polypeptide. Point out the specific side-chain interactions that could occur in this polypeptide by labelling the polypeptide. Defend your answer as to why your polypeptide should assume such final shape. Only accurate drawing need

Shown below is the structure of a polypeptide with the pK, values of its acidic hydrogens. pK = = 10.1 H OH pK, = 9.2 H. pKa = 2.1 H. N-H pK, = 6.0 pKa = 3.9 1. How many peptide bonds are present in one molecule of the polypeptide? [ Select ] II. Over what pH range would this molecule predominantly exist in a state that has a net charge of zero? [ Select ] ZI

Please, need help with the explanation and diagram. The structure and properties of poly peptides: A) Describe the type of bonding that would occur when three amino acid monomers (include a diagram of the amino acids) form a tripeptide and describe how such bonds could be formed. B) During the period of Chemical Evolution, what is the significance of the structure of the polymer formed? (Include a diagram)

Identify the following types of biomolecules and label and identify the functional groups

Please answer the question 1 and 2 <3 I will give you a thumbs up :) 1.What type of bonds stabilizes the quaternary structure of proteins? * A. Peptide bond B. Electrostatic interactions C. Hydrogen bonds D. Disulfide bridges E. Hydrophobic bonds2.  A new drug is developed which selectively cleaves covalent bonds between two sulfur atoms of non-adjacent amino acids in a polypeptide chain. Which level of protein structure in affected molecules would be most directly affected by the drug? * A. Primary B. Secondary C. Tertiary D. Quaternary

Are these amino acids classified correct?

What are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved. The molecule considered is a protein: pancreatic amylase.