Generic tertiary folding properties of proteins on mesoscopic scales

1 A simple model for a parallel p helix lattice protein 

As a first example we consider the conformational transitions accompanying the tertiary folding behavior of the sequence of hydrophobic (H) and polar residues (P) 

It is a nice example because, despite the simplicity and limitations of the model, it shows transition features that are very characteristic for heteropolymer folding and apply, in similar form, to realistic proteins as well. In the following, we will discuss the transition behavior in detail by means of statistical canonical analysis, which will give us some general insight into the interpretation of conformational transitions of proteins as finite-size variants of structural phase transitions. 

The average structural properties at finite temperatures can be characterized well by the mean end-to-end distance and the mean radius of gyration (iigyr)(7), as shown 

Generic tertiary foiding properties of proteins on mesoscopic scales 

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