More compact protein globules exhibit slower folding rates

Oxana V. Galzitskaya, Danielle C. Reifsnyder, Natalya S. Bogatyreva, Dmitry N. Ivankov, Sergiy O. Garbuzynskiy

Research output: Contribution to journalArticlepeer-review

37 Citations (Scopus)


We have demonstrated that, among proteins of the same size, α/β proteins have on the average a greater number of contacts per residue due to their more compact (more "spherical") structure, rather than due to tighter packing. We have examined the relationship between the average number of contacts per residue and folding rates in globular proteins according to general protein structural class (all-α, all-β, α/β, α+β). Our analysis demonstrates that α/β proteins have both the greatest number of contacts and the slowest folding rates in comparison to proteins from the other structural classes. Because α/β proteins are also known to be the oldest proteins, it can be suggested that proteins have evolved to pack more quickly and into looser structures.

Original languageEnglish
Pages (from-to)329-332
Number of pages4
JournalProteins: Structure, Function and Genetics
Issue number2
Publication statusPublished - 1 Feb 2008
Externally publishedYes


  • Compactness
  • Number of contacts per residue
  • Protein packing
  • Structural class


Dive into the research topics of 'More compact protein globules exhibit slower folding rates'. Together they form a unique fingerprint.

Cite this