Lesk: Introduction to Genomics 
Answers to end-of-chapter exercises
Figures from the bookLesk: Introduction to Genomics
Chapter 01
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Page 12, Fig 1.9
The structure of adult human haemoglobin. The protein contains four polypeptide chains -
two α-subunits and two β-subunits - each binding a haem group. Cylinders represent α-helices. Spheres represent atoms of the haem groups. (Each picture of a macromolecule illustrates an entry in the Protein Data Bank (PDB), described in Chapter 4. PDB identifiers are four-character codes. This figure is based on PDB entry 1HHO.)
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Page 20, Fig 1.14
The structure of DNA. The two helical strands wind around the outside of the
structure. The bases are inside, stacked like the treads of a staircase with their planes
perpendicular to the axis of the double helix. The bases are visible through the major and minor grooves and are thereby accessible for interaction with proteins. This picture shows a stereo pair, most easily viewed with a standard stereo viewer or lorgnette.
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Page 43, Fig 1.24
The immunological distinction between 'self' and 'non-self' resides in the proteins of the major histocompatibility complex (MHC) and their interaction with T-cell receptors. This picture shows a human T-cell receptor in a complex with a class I MHC protein and a viral peptide. MHC proteins have broad specificity, each binding many peptides including those of self and nonself origin. Cell surfaces contain large numbers of MHC-peptide complexes, among which those binding foreign peptides are a small minority. T-cell receptors, in contrast, have a narrow specificity and pick out the complexes containing foreign peptides [2CKB].
The extracellular fragment of the T-cell receptor, at the top of the picture, contains two chains - Vα-Cα (yellow) and Vβ-Cβ (blue). The MHC protein consists of two polypeptide chains, one containing the peptide-binding fragment (red) and a single-domain
β2-microglobulin (green). The peptide sits between the T-cell receptor and the MHC protein.
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