BIO130H1 Chapter Notes - Chapter 2: Globular Protein, Myoglobin, Peptide
31
BIO130H1 Full Course Notes
Verified Note
31 documents
Document Summary
Myoglobin: the first globular protein whose tertiary structure was determined. The polypeptide chains of globular proteins are folded and twisted into complex shapes. Distant points on the linear sequence of amino acids are brought next to each other and linked by various types of bonds. The first glimpse at the tertiary structure of a globular protein came in 1957 through the x ray crystallographic studies of john. Kendrew and his colleagues at cambridge university using x ray: the protein they reported on was myoglobin diffraction patterns. The first report on the structure of myoglobin provided a low . The earliest crude profile of myoglobin revealed eight rod like stretches of (cid:573) helix ranging from 7 to 24 amino acids in length the polypeptide chain are in the (cid:573) helical conformation: no (cid:574) sheet was found. Subsequent analyses of myoglobin using additional x ray diffraction data provided a much more detailed picture of the molecule.
