BCH210H1 Lecture Notes - Lecture 3: Hydrophile, Globular Protein, Hemoglobin

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Stavroula Andreopoulos

Document Summary

Primary structure is simply the amino acid sequence joined together by peptide bonds (amide linkages), creating a linear array. Linear polypeptide folds up into a three-dimensional structure that is essential to the functional state. Levels of protein structure: primary (1 ): linear amino acid sequence, secondary (2 ): periodic, repetitive units. Single amino acid changes can alter the folding pattern and final 3d pattern and thus function. There are two polypeptide chains (a and b) Start from n terminal all the way to the cooh terminal. Side chains need to minimize steric clashes: helices can be right-handed or left handed, most commonly right-handed. In a linear sequence, these are far apart, but in the helix, they come together: distance in h-bond is about 1. 5 angstroms. Intramolecular h-bonds stabilize the structure: n-h group of reside i donates hydrogen back to. Interact with the surrounding environment (water or protein)