@text "SECONDARY STRUCTURE -- THE ALPHA-HELIX" There are two basic structural features that can be found in proteins. One of these secondary structure elements is the alpha-helix, which is formed by a relatively short stretch of consecutive amino acids within the protein. Alpha-helices are very common and can be found, usually more than once, in many proteins. They can contain 4 amino acids to over 40 (the average is 10). They are held in this spiral shape by hydrogen bonds, which involve the mainchain carbonyl oxygen of residue "i" and the mainchain nitrogen of residue "i+4". One complete turn in an alpha-helix requires 3.6 residues. The tendency of a sequence of amino acids to form one structure over another is determined by the types of amino acids in the sequence. Since proteins fold up in aqueous solution based on the properties described in the amino acid kinemage, the general structure of proteins is one that keeps the majority of hydrophilic amino acids facing out toward the aqueous solution and keeps hydrophobic amino acids facing in toward the core of the protein, away from the water. This core region is known as the hydrophobic core and is an important feature in protein structure. Of course, there are proteins found in cell membranes that require a predominance of hydrophobic residues on the exterior, for solubility in this lipid environment. Most alpha-helices appear at the periphery of proteins, so they usually contain one side of hydrophilic amino acids and one side of hydrophobic, giving them 'amphiphilic' (or amphipathic) character. @kinemage 1 @caption The start-up view shows an eleven-residue alpha-helix from the end-on perspective. Repeatedly click on 'ANIMATE' to highlight the residues in one complete turn of the helix. Select view2 for a side view of the helix. Turn on 'Hydrophilic' and 'Hydrophobic' to see the distribution of residues, responsible for the amphiphilic character of the helix. 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