The plan of this thesis is as follows: in the next chapter (chapter 1)
we review the main properties of globular proteins, in particular focusing
on the state of the art of protein folding and design. Then we describe in
detail the simple model for folding adopted throughout the present work
(chapter 2). Chapter 3 shows the further modeling introduced to handle the
specific subject of disordered proteins, with full explanation of all parameters
used and with some possible interpretation of the results obtained.
In the last chapter of this work (chapter 4) we present a study on the
near equilibrium dynamics of two small proteins in the family of truncated
hemoglobins, developed under the framework of a Gaussian network approach.
