Folding, of proteins

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The examples of modelling discussed in section C2.5.2 and section C2.5.3 are meant to illustrate tlie ideas behind tlie tlieoretical and computational approaches to protein folding. It should be borne in mind tliat we have discussed only a very limited aspect of tlie rich field of protein folding. The computations described in section C2.5.3 can be carried out easily on a desktop computer. Such an exercise is, perhaps, tlie best of way of appreciating tlie simple approach to get at tlie principles tliat govern tlie folding of proteins. 

Anfinsen C B 1973 Prinoiples that govern the folding of protein ohains Science 181 223-30... 

CB Anfinsen. Principles that govern the folding of protein chains. Science 181 223-238, 1973. 

Similar residues in the cores of protein structures especially hydrophobic residues at the same positions, are responsible for common folds of homologous proteins. Certain sequence profiles of conserved residue successions have been identified which give rise to a common fold of protein domains. They are organized in the smart database (simple modular architecture research tool) http //smait.embl-heidelberg.de. 

Sequence conservation is, in general, much weaker than structural conservation. There are proteins, which are clearly not related in sequence but are closely related in 3D-stmcture and fold, like heamoglobin and myoglobin, which have similar functions. In many proteins, fold elements like 4-helical bundles are repeated. Classifications of known structural folds of proteins are organized in the SCOP or CATH database see e.g., http //scop.mrc-lmb.cam.ac.uk/scop/. 

The resulting insight of MD is ciucial in studies of fast photo biological reactions and instructive in cases of slower processes. Very slow processes like folding of proteins cannot be traced by MD, because folding takes a time range between 20 ms and 1 h. 

Ethylammoniinn niirate, l H jf HjNH tNOj, was the first limit liquid to he discovered. Its melting point of 12°C was reported in 1914 and it has since been used as a nonpolluting solvent for organic reactions and for facilitating the folding of proteins. 

The role of chaperone proteins in the folding of proteins is presented, and a model describing budding... 

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