Conformational ensembles

This movie depicts the 3-D structures of each of the representative conformations of the Markov State Model of Pin1 WW domain.

In computational chemistry, conformational ensembles, also known as structural ensembles, are experimentally constrained computational models describing the structure of intrinsically unstructured proteins.[1][2] Such proteins are flexible in nature, lacking a stable tertiary structure, and therefore cannot be described with a single structural representation.[3] The techniques of ensemble calculation are relatively new on the field of structural biology, and are still facing certain limitations that need to be addressed before it will become comparable to classical structural description methods such as biological macromolecular crystallography.[4]

  1. ^ Fisher CK, Stultz CM (June 2011). "Constructing ensembles for intrinsically disordered proteins" (PDF). Current Opinion in Structural Biology. (3). 21 (3): 426–31. doi:10.1016/j.sbi.2011.04.001. hdl:1721.1/99137. PMC 3112268. PMID 21530234.
  2. ^ Varadi M, Kosol S, Lebrun P, Valentini E, Blackledge M, Dunker AK, Felli IC, Forman-Kay JD, Kriwacki RW, Pierattelli R, Sussman J, Svergun DI, Uversky VN, Vendruscolo M, Wishart D, Wright PE, Tompa P (January 2014). "pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins". Nucleic Acids Research. 42 (Database issue): D326-35. doi:10.1093/nar/gkt960. PMC 3964940. PMID 24174539.
  3. ^ Dyson HJ, Wright PE (March 2005). "Intrinsically unstructured proteins and their functions". Nature Reviews. Molecular Cell Biology. 6 (3): 197–208. doi:10.1038/nrm1589. PMID 15738986. S2CID 18068406.
  4. ^ Tompa P (June 2011). "Unstructural biology coming of age". Current Opinion in Structural Biology. 21 (3): 419–25. doi:10.1016/j.sbi.2011.03.012. PMID 21514142.