Ontology highlight
ABSTRACT:
SUBMITTER: Haliloglu T
PROVIDER: S-EPMC1305212 | biostudies-literature | 2005 Mar
REPOSITORIES: biostudies-literature
Haliloglu Turkan T Keskin Ozlem O Ma Buyong B Nussinov Ruth R
Biophysical journal 20041213 3
The underlying physico-chemical principles of the interactions between domains in protein folding are similar to those between protein molecules in binding. Here we show that conserved residues and experimental hot spots at intermolecular binding interfaces overlap residues that vibrate with high frequencies. Similarly, conserved residues and hot spots are found in protein cores and are also observed to vibrate with high frequencies. In both cases, these residues contribute significantly to the ...[more]