Protein

Description

-Structure of Amino Acid -Synthesis and breakdown of peptide bonds -Levels of protein structure -Structure an function of globular proteins -Properties and functions of fibrous proteins
Dean Lundie
Mind Map by Dean Lundie, updated more than 1 year ago
Dean Lundie
Created by Dean Lundie over 8 years ago
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Resource summary

Protein
  1. Amino Acids
    1. 'Monomers of Proteins'
      1. Carbon, Hydrogen, Oxygen,Nitrogen
        1. Structure
          1. Carboxyl Group (-COOH)
            1. Amino Group (-NH3)
              1. Difference between amino acids is caused by the variable group (R)
              2. The molecules that make up proteins
              3. Peptide Bonds
                1. Formed by condensation reaction between two amino acids
                  1. Dipeptide
                    1. Two amino acids bonded together
                    2. Polypeptide
                      1. Multiple Amino Acids bonded together
                    3. Primary Structure
                      1. Held by Peptide bonds
                        1. Polypeptides
                          1. The protein is determined by the sequence of amino acids in the polypeptide chain
                            1. Different proteins have different sequences
                            2. Secondary Structure
                              1. Polypeptide chain folds due to hydrogen bonds forming between amino acids
                                1. Alpha Helix
                                  1. Beta-pleated Sheet
                                    1. Held together by hydrogen bonds between the amino group of one amino acid and the carboxyl group of another amino acid further down the chain
                                    2. Tertiary Structure
                                      1. Secondary structures can fold further to make complex 3D structures
                                        1. Held together by...
                                          1. Hydrogen Bonds
                                            1. Ionic Bonds
                                              1. Disulfide Bonds
                                                1. Hydrophobic and Philic interactions
                                              2. Quaternary Structure
                                                1. Several Polypeptide chains bonded
                                                  1. The way these multiple chains are assembled
                                                  2. Bonds in Tertiary Structure
                                                    1. Hydrogen
                                                      1. Weak bonds form between +ve charged hydrogen atoms in some R groups and -ve charged atoms in another on the chain
                                                      2. Hydrophobic/philic
                                                        1. Hydrophobic R groups clump together and push Hydrophilic R groups to the outside
                                                        2. Disulfide
                                                          1. When two molecules of the amino acid cysteine get close, the two sulphur atoms bond
                                                          2. Ionic
                                                            1. Attraction between +ve R groups and -ve R groups on different parts of the molecule
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