BIOLOGY 2B03 Lecture Notes - Lecture 2: Beta Sheet, Carboxylic Acid, Protein Folding
8 Dec 2018
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Definition: the local chemical interactions that fold a protein that create a conformation of a portion of the polypeptide. The secondary structure is the periodic folding of the polypeptide chain into conserved arrangements. These structures are determined by h- bonding between the non-variable side groups of the amino acids (aminos and carboxyl groups). Neighbouring amino acids are connected through peptide bonds. But hydrogen bonds (green dotted lines) connect other amino acid residues to form the alpha helix. Hydrogen bond with an amino acid residue 4 positions away. This helix pattern is found exactly the same in all proteins since the variable. R groups are not involved in determining the structure of the alpha helix. The r groups determine the characteristics of the alpha helix, as the alpha helix can be hydrophilic, hydrophobic, or even amphipathic. Structure is defined by the pattern of hydrogen bonding (dotted lines) between the carboxyl and amino groups of the residues.
