Global characteristics of protein sequences and their implications

S. Rackovsky

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Computational studies of the relationships between protein sequence, structure, and folding have traditionally relied on purely local sequence representations. Here we show that global representations, on the basis of parameters that encode information about complete sequences, contain otherwise inaccessible information about the organization of sequences. By studying the spectral properties of these parameters, we demonstrate that amino acid physical properties fall into two distinct classes. One class is comprised of properties that favor sequentially localized interaction clusters. The other class is comprised of properties that favor globally distributed interactions. This observation provides a bridge between two classic models of protein folding - the collapse model and the nucleation model - and provides a basis for understanding how any degree of intermediacy between these two extremes can occur.

Original languageEnglish
Pages (from-to)8623-8626
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number19
StatePublished - 11 May 2010
Externally publishedYes


  • Proteomics
  • Sequence analysis


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