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Proteins
Proteins are either fibrous or globular in structure
Fibrous proteins, such as keratin and collagen, are structural build muscles, hair, nails, ligaments, tendons, eyeballs, connective tissue etc.
Globular proteins usually metabolic and help carry out chemical reactions
Enzymes are globular proteins, as well as proteins embedded in cell membranes
Amino Acids and Peptides
All proteins begin as strings of amino acids, bonded together by peptide linkages
This is another example of dehydration synthesis
The bond forms between the amino group and the carboxyl group of adjacent amino acids
The First Amino Acid Sequence
Sanger wrote in his 1952 review: It has frequently been suggested that proteins may not be
pure chemical entities but may consist of mixtures of closely related substances with no absolute unique structure. The chemical results obtained so far suggest that this is not the case, and that a protein is really a single chemical substance, each molecule of one protein being identical to every other molecule of the same pure protein.
He used HCL to hydrolyze insulin into small peptides He then used a combination of chromatography and
electrophoresis to separate the small peptides and identify their chemical structure
He was the first person to think of proteins as stable chemicals and one the first of two Nobel prizes for this discovery
Polypeptides – Primary Structure
Amino acids form long chains called polypeptides There are 20 amino acids and we need to consume all 20 at once to
build proteins (8 are essential from the diet and 12 are manufactured) Any unused protein that we consume is deaminated (amino group is
removed) and converted into a lipid The peptide is considered to be the primary structure of a protein –
the sequence of amino acids and a non-functional chain
Secondary Structure α-helix
This is one possible secondary structure, the alpha helix (α-helix)
The polypeptide coils and is held in place with hydrogen bonds between the NH and C=O of the peptide bond
Seconday Structure β pleated sheet
Polypeptides can also form pleated sheets (p. 44)
Hydrogen bonds form between adjacent polypeptides at the NH and C=O
The secondary structure is dependent on the initial primary structure
the NH and C=O groups must line up correctly to form the hydrogen bonds
The alpha helix in keratin
Many alpha helicies bind together to form fibrils which build up the structure of hair
Tertiary Structure
Once the secondary structures are complete, proteins fold into 3 dimensional shapes based on intermolecular interactions, ionic bonds and covalent bonds defined by the primary structure
Covalent bonds between sulfhydryl groups form disulfide bridges
Hydrogen bonds, dipole-dipole interactions and hydrophobic interactions produce characteristic shapes
Ionic bonds form between positive and negative charged functional groups