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Protein Structure 1 Notes

Pharmacology Notes > BIOL10212 Biochemistry Notes

This is an extract of our Protein Structure 1 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 5 (12/02/2018)

Proteins: Primary and Secondary Structures
Protein Primary Sequences

The linear sequence of amino acids is around made up of 30-1000+ amino acids.
These amino acids form unique sequences to code for proteins.

The primary sequences of proteins can be compared against an entire database of sequences (for example the Swiss-Prot database) in order to reveal relationships, like similar protein folding, their function or if whether they're evolutionarily related.
This is called 'Bioinformatics'.

Peptide bonds link Amino Acids in Proteins

Condensation of the α-carboxyl of one amino acid with the
α-amino of another gives rise to a Peptide bond (which is a type of Amide bond).

Amino acid 'residues' compose peptide chains.
For example, the Ebola virus small secreted glycoprotein has 364 residues.

Peptide chains are numbered from the N (Amino) terminus to the C (Carboxyl) terminus.

The repeating N-Cα-C unit constitutes the backbone of the peptide chain.

The 4 levels of Protein Structure
 Primary structure - Linear amino acid sequence.
 Secondary structure - These contain regions of regularly repeated conformations of the peptide chain, such as α-helices and β-strands (local folding).
 Tertiary structure - These describe the shape of the fully folded polypeptide chain.
 Quaternary structure - This is the arrangement of two or more polypeptide chains which combines into a multisubunit molecule.

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