BIO-1801 Lecture Notes - Lecture 6: Alpha Helix, Protein Folding, Chemical Polarity

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Composed of carbon, hydrogen, oxygen, nitrogen, and small amounts of other elements, notably sulfur. Amino acids are the monomers: common structure with variable r-group, 20 amino acids, side-chain (or r-group) determines structure function. Joined by dehydration or condensation reaction: peptide bond, forms polypeptides, proteins are made up of 1 or more polypeptides. Recognize two amino acids linked together by peptide bond. Primary: amino acid sequence, determined by genes (precise sequence of nucleotides on a dna molecule) Secondary: chemical and physical interactions cause folding, repeating patterns, helices and pleated sheets. Key determinants of a protein"s characteristics: random coiled regions . Not helix or pleated sheet. Tertiary: folding gives complex three-dimensional shape, final level of structure for single polypeptide chain. Quaternary: found in some proteins but not all, made up of 2 or more polypeptides. Hydrogen bonds (holds alpha helix in place) Many cellular processes involve steps in which two or more different proteins interact with each other.

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