20.1: functions of proteins
Be able to list the 7 classes of proteins and their function in the cell or body.
20.2 amino acids
Draw the structure of amino acids
Given an amino acid, classify it as non-polar, polar, acidic, or basic.
Given an amino acid, determine if it is a D or L- amino acid.
Draw the Fischer projections of amino acids.
20.3 amino acids as acids and bases
Draw the ionic form of an amino acid at the pH above the pI, at the pI and below the pI.
Briefly, summarize the process of electrophoresis.
Given three or four amino acids, their pIs, and the pH of the buffer, determine the movement of the amino acids on an electrophoresis gel.
20.4 formation of peptides
Draw the structure of a dipetide from the zwitterions of two or more amino acids
Identify a peptide bond
Name the peptide, given two or three peptides in a polypeptide.
20.5 protein structure: primary and secondary levels
Identify the primary and secondary structures of a protein.
Describe the differences between 1° and 2° structures: what bonds hold each structure in place?
20.6: Protein structure: tertiary and quaternary levels
Be able to distinguish between 3° and 4° structures of a protein
Distinguish between the 5 cross links in a tertiary structures
Be able to label the cross links on a generic protein.
Distinguish between globular and fibrous proteins.
Name 1 quaternary structure.
20.7 protein hydrolysis and denaturation
Describe the process of denaturation of proteins
Distinguish between the 5 denaturation processes of proteins
Describe hydrolysis of a protein.
Discuss the effects of denaturation on a generic protein.
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INTERPOLATION 41 CHAPTER 5 INTERPOLATION THIS CHAPTER SUMMARIZES POLYNOMIAL
PREPARING FOR PRODUCTION DEPLOYMENT 219 CHAPTER 4 DESIGNING A
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