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Lecture

Chapter 9-2.docx

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Department
Biology
Course
BIOL 2000
Professor
Joseph Rasmussen
Semester
Winter

Description
Chapter 9-2 Tertiary structure  The overall 3D shape of the entire protein o Globular proteins  Has alpha-helical regions coming together in 3D space  Where does a small molecule bind? o Heme  Where are the precise positions of the atoms in 3D space o We will know exactly what it is made up of Quaternary structure  Several proteins coming together  Intercations between multiple polypeptides  Hemoglobin complex o For oxygen transport o Four separate polypeptides for the complex  2 of each alpha and beta  Heterotetramer  dimer o 2  tetramer o 4  Homo- o identical subunits  Hetero- o different subunits (different polypeptides) The genetic code  How id the sequence in DNA eventually converted into linear amino acid sequence (primary structure of proteins? o How is the mRNA template read?  1) How many nucleotides specify one amino acid in a protein? Condon  Length of mRNA sequence that specifies one amino acid  Codon length possibilities o 1 nt= 4 combinations (4 amino acids) o 2 nt = 4x4 = 16 amino acids o 3 nt = 4x4x4 = 64 amino acids (maximally)  only need 20 to specify  Codons are 3 nt long  How are codons read? o Overlapping genetic code  One nt affects amino acid composition at more then one position o Non-overlapping  Each nt is only part of one codon o Dependent on the reader
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