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Protein Structure 2 Notes

Pharmacology Notes > BIOL10212 Biochemistry Notes

This is an extract of our Protein Structure 2 document, which we sell as part of our BIOL10212 Biochemistry Notes collection written by the top tier of University Of Manchester students.

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Biochemistry - Lecture 6 (15/02/2018)

Tertiary and Quaternary Structure
Loops and Turns

Loops and Turns connect α helices and β strands and allow a peptide chain to fold back on itself to form a compact structure.

Loops - Often contain hydrophilic residues and are found on protein surfaces.

Turns - Loops containing 5 residues or less.

Tertiary Structure of Globular Proteins

Tertiary structure = A closely packed three-dimensional form of a protein.

Each protein folds its polypeptide chain into a tertiary structure which is specifically adapted for a particular biological function.

Amino acids far apart in the primary structure can be brought together in a tertiary structure.

Amino acids distribute themselves so that non-polar side chains are found on the interior and polar/charged side chains are displayed on the exterior (not trans-membrane proteins).

Protein tertiary structures are stabilised primarily by non-covalent interactions between side chains. Disulfide bridges can also stabilise tertiary structure.

Myoglobin - (O2 binding molecule in Red Blood Cells)
 Yellow = Non-polar.
 Blue = Charged.

Turns: 4 x 3.6 = Around 14 Amino Acids.

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