BIO130H1 Lecture 1: BIO130 Textbook Notes Chp 3
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BIO130H1 Full Course Notes
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Document Summary
The shape of a protein is speciied by its amino acid sequence. Proteins (polypepides) have a polypepide backbone (repeaing atoms along polypepide chain) Noncovalent bonds involve the polypepide backbone and atoms in amino acid side chain. Nonpolar side chains tend to cluster into the interior of a molecule, where polar groups arrange near outside of molecule to take part in hydrogen bonding with water and other polar molecules. Polar amino acids buried within the protein are usually hydrogen-bonded to other polar amino acids or to the pepide backbone. Proteins fold into a conformaion of lowest energy. Treatment with certain solvents, which disrupt the noncovalent interacions holding the folded chain together, unfolds, or denatures, a protein, but when solvent removed, protein can renature itself. Amino acid sequence contains all informaion needed to determine 3d structure of protein (helps us understand cell funcion) Molecular chaperones help protein fold and prevent exposed hydrophobic parts from interacing with each other to form protein aggregates.
