A hierarchical protein folding scheme based on the building block folding model.

Nurit Haspel*, Gilad Wainreb, Yuval Inbar, Hui Hsu Tsai, Chung Jung Tsai, Haim J. Wolfson, Ruth Nussinov

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


The building block protein folding model states that the native protein structure is the product of a combinatorial assembly of relatively structurally independent contiguous parts of the protein that possess a hydrophobic core, i.e., building blocks (BBs). According to this model, our group proposed a three-stage scheme for a feasible time-wise semi ab-intio protein structure prediction. Given a protein sequence, at the first stage of the prediction scheme, we propose cutting the sequence into structurally assigned BBs. Next, we perform a combinatorial assembly and attempt to predict the relative three-dimensional arrangement of the BBs. In the third stage, we refine and rank the assemblies. The scheme has proven to be very promising in reducing the complexity of the protein folding problem and gaining insight into the protein folding process. In this chapter, we describe the different stages of the scheme and discuss a possible application of the model to protein design.

Original languageEnglish
Pages (from-to)189-204
Number of pages16
JournalMethods in Molecular Biology
StatePublished - 2007


FundersFunder number
National Cancer InstituteZ01BC010440


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