BIO206H5 Study Guide - Midterm Guide: Transcription Factor Ii D, Transcription Factor Ii H, Stem-Loop
Document Summary
Chapter 4 the shape and structure of proteins. Protein shape specified by amino acid sequence; nucleotides linked by covalent peptide bonds. Noncovalent bonds that help proteins maintain their shape: hydrogen bonds, electrostatic attractions, van der waals attractions, hydrophobic interactions. Final folded structure (conformation) is generally the shape that gives the protein the lowest free energy. Denatured protein can refold and renature itself indicating that all the information needed to specify the 3d shape of a protein is in its amino acid sequence. Incorrectly folded proteins can form aggregates that can damage cells and even whole tissues aggregates can convert normal proteins into aggregates. Protein folding is generally assisted by proteins called molecular chaperones. Most proteins are formed from multiple domains. Hydrogen bonds between n-h and c=0 groups of backbone. H-bond between every 4th amino acid, linking c=o of one aa to the n-h of another aa, helix with complete turn every 3. 6 aa.
