MCB 250 Lecture Notes - Lecture 5: Amine, British Association For Immediate Care, Crystallography

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Salt bridges: can form between the oppositely charged side chains of residues within proteins from a combination of two relatively weak noncovalent interactions: Protein structure can be described at four levels. Primary structure: the sequence of amino acid residues in the polypeptide chain, an amino acid in a protein is called a residue since it has lost water and is no longer an amino acid. Secondary structure: the local conformation of a protein"s polypeptide chain the 3d arrangement of a short stretch of amino acid residues. Involves hydrogen bonding between c=o and nh groups that are part of the peptide backbone. C=o: the properties of the helix are defined by the amino acid side chains. Example an amphipathic helix and the coiled-coil : not all amino acids are favorable for alpha helices, malek are favored, p is a breaker, g is disfavored. Tertiary structure: the usually compact, three-dimensionally folded arrangement that the polypeptide chain adopts under physiological conditions.

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