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Jillian Cheong

on 5 October 2010

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Transcript of Proteins

Protein structure Bonds:
Disulphide bridges
Ionic interactions
Hydrogen bonds
Hydrophobic interactions Liner sequence of amino acid residues joined together by peptide bonds refers to the
of amino acids in the polypeptide beta sheet alpha helix Myoglobin a globular protein found in skeletal muscles. Functions as a reservoir for oxygen within muscle cells Primary structure:
a single peptide chain, 153 amino acids long

Secondary structure:
8 segments of an alpha helix

Tertiary structure:
complex globular structure H-bonds between C=O and N-H of peptide bonds Hydrophobic interactions between non-polar amino acids in the interior of the molecule stabalizes the molecule
Charged and polar amino acid residues located almost exclusively on the surface form weak H-bonds with water H-bonds between C=O and N-H of peptide bonds interaction between more than one poly peptide chain to form an intact functional protein Haemoglobin A globular protein found in RBCs. Important in the transport of oxygen. 4 polypeptide chains (2alpha and 2 beta) held together by hydrogen bonds, hydrophobic interactions and charge interactions between R groups Organized into:
Quaternary e.g. e.g. Denaturation of proteins loss of 3dimentional structure and therefore functions heat high heat breaks h-bonds
Full transcript