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Introduction

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BSc Protein Form and Function Mind Map on Introduction, created by Jen Harris on 24/05/2013.
Jen Harris
Mind Map by Jen Harris, updated more than 1 year ago
Jen Harris
Created by Jen Harris almost 11 years ago
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Resource summary

Introduction
  1. Genetics
    1. 5'-3' orientation
      1. N terminal --> C terminal
      2. Protein chains always begin with Met
      3. Amino acids
        1. Negative side chains
          1. Aspartic acid
            1. Glutamic acid
            2. Positive side chains
              1. Arginine
                1. Lysine
                  1. Histidine
                  2. Uncharged polar side chains
                    1. Asparagine
                      1. Glutamine
                        1. Serine
                          1. Threonine
                            1. Tyrosine
                            2. Nonpolar side chains
                              1. Alanine
                                1. Glycine
                                  1. Valine
                                    1. Leucine
                                      1. Isoleucine
                                        1. Proline
                                          1. Phenylalanine
                                            1. Methionine
                                              1. Tryptophan
                                                1. Cysteine
                                                2. Handedness
                                                  1. L-type
                                                    1. CORN crib
                                                3. Proteins
                                                  1. Polymers of amino acid monomers
                                                    1. Peptide bonds
                                                      1. Properties
                                                        1. Shared
                                                          1. Unique to each amino acid
                                                          2. Secondary structure
                                                            1. Alpha helix
                                                              1. Beta sheet
                                                                1. Determinants
                                                                  1. Backbone bonds
                                                                    1. Phi angles
                                                                      1. Psi angles
                                                                      2. Hydrogen bonds between main chain atoms
                                                                      3. Supersecondary structure
                                                                        1. The arrangement of secondary structural regions
                                                                      4. Tertiary structure
                                                                        1. The way in which secondary structures associate
                                                                        2. Quaternary structure
                                                                          1. The overall protein molecule
                                                                            1. Larger association
                                                                              1. Folding
                                                                              2. Bond types
                                                                                1. Backbone-backbone
                                                                                  1. Hydrogen bonds between atoms of two peptide bonds
                                                                                  2. Backbone-side chain
                                                                                    1. Hydrogen bond between atoms in peptide bond and amino acid side chain
                                                                                    2. Side chain-side chain
                                                                                      1. Hydrogen bonds between two amino acid side chains
                                                                                      2. Van der Waals
                                                                                        1. Electrostatic attraction
                                                                                        2. Structure types
                                                                                          1. Transmembrane
                                                                                            1. Bacteriorhodopsin
                                                                                            2. Globular
                                                                                              1. Myoglobin
                                                                                              2. Fibrous
                                                                                                1. Collagen
                                                                                            3. Chaperonins
                                                                                              1. Specialised proteins which protect folding
                                                                                                1. Cylindrical
                                                                                                  1. Unfolded protein enters cylinder from one end
                                                                                                    1. Cap attaches to that end
                                                                                                      1. Cylinder changes shape
                                                                                                        1. Hydrohilic environment conducive to folding created
                                                                                                  2. Properly folded proteins released
                                                                                                2. Influences on folding
                                                                                                  1. Size
                                                                                                    1. Amino acid content
                                                                                                      1. Hydrophilic/hydrophobic
                                                                                                      2. Strength of intramolecular interactions
                                                                                                        1. Number of S-S bonds
                                                                                                          1. Domain architecture
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