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Protein folding of the SAP domain, a naturally occurring two‐helix bundle
Author(s) -
Dodson Charlotte A.,
Arbely Eyal
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.06.002
Subject(s) - helix bundle , protein folding , native state , chemistry , helix (gastropod) , contact order , folding funnel , crystallography , folding (dsp implementation) , biophysics , lattice protein , phi value analysis , protein structure , biochemistry , downhill folding , biology , ecology , snail , electrical engineering , engineering
The SAP domain from the Saccharomyces cerevisiae Tho1 protein is comprised of just two helices and a hydrophobic core and is one of the smallest proteins whose folding has been characterised. Φ‐value analysis revealed that Tho1 SAP folds through a transition state where helix 1 is the most extensively formed element of secondary structure and flickering native‐like core contacts from Leu35 are also present. The contacts that contribute most to native state stability of Tho1 SAP are not formed in the transition state.