The paper discusses the role of local structural preferences of protein seg
ments in the folding of proteins. First a short overview of the local, seco
ndary structures detected in peptides, protein fragments, denatured protein
s and early folding intermediates is given. Next the discussion of their ro
le in protein folding is presented based on recent literature and data obta
ined in our laboratory. In conclusion it is pointed out that, during foldin
g, local structures populated at low levels in denatured state may facilita
te the crossing of the folding transition state barrier, and consequently a
ccelerate the rate limiting step in folding. However, the data show that th
is effect does not follow simple rules.