BIO206H5 Chapter Notes - Chapter 4: Nuclear Magnetic Resonance, X-Ray Crystallography, Antifreeze Protein
Document Summary
Shape of protein is specified by its amino acid sequence. Protein - referred to as polypeptides/ polypeptide chains (arranged in amino acid sequence) Proteins fold into a conformation of lowest energy. Denatured proteins can renature if denaturing solvent is removed. H bonds within a protein molecule help stabilize its folded shape. Molecular chaperones - assist in protein folding in living cells. Proteins come in a wide variety of complicated shapes. Average of 50 to 2000 amino acids long. Either the use of x-ray crystallography or nuclear magnetic resonance (nmr) spectroscopy can we predict the precise folding pattern of a protein. Protein domain - part of a protein, 100-250 amino acids. Displayed as: polypeptide backbone model - shows overall organization of polypeptide in a clean way to compare structures of related proteins ribbon model - easy way to visualize secondary structures such as helices and . Shows how the protein might look to a small molecule (ex.
