Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module.


An analysis of the folding of the 94 residue tenth fibronectin type III (fnIII) domain of human fibronectin (FNfn10) is presented. Use of guanidine isothiocyanate as a denaturant allows us to obtain equilibrium and kinetic data across a broad range of denaturant concentrations that are unavailable in guanidine hydrochloride. Equilibrium unfolding experiments show that FNfn10 is significantly more stable than has been reported previously. Comparison of equilibrium and kinetic parameters reveals the presence of an intermediate that accumulates at low denaturant concentrations. This is the first demonstration of three-state folding kinetics for a fnIII domain. We have previously shown that a homologous domain from human tenascin (TNfn3) folds by a two-state mechanism, but this does not necessarily indicate that the two proteins fold by different folding pathways. Study holds ProTherm entries: 8084, 8085, 8086 Extra Details: FNfn10; tenth fnIII domain of fibronectin

Submission Details

ID: f4dhpfV8

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:35 p.m.

Version: 1

Publication Details
Cota E;Clarke J,Protein Sci. (2000) Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module. PMID:10739253
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Ribonuclease P00648 RNBR_BACAM
97.3 Ribonuclease P35078 RN_BACCI
100.0 Fibronectin P02751 FINC_HUMAN
94.0 Fibronectin Q28275 FINC_CANLF
92.1 Fibronectin Q28377 FINC_HORSE
90.9 Fibronectin Q91400 FINC_NOTVI
100.0 Tenascin P24821 TENA_HUMAN
95.6 Tenascin Q29116 TENA_PIG
96.8 Fibronectin P07589 FINC_BOVIN