Near-complete 1H, 13C, 15N resonance assignments of dimethylsulfoxide-denatured TGFBIp FAS1-4 A546T

Biomol NMR Assign. 2016 Apr;10(1):25-9. doi: 10.1007/s12104-015-9630-2. Epub 2015 Aug 15.


The transforming growth factor beta induced protein (TGFBIp) is a major protein component of the human cornea. Mutations occurring in TGFBIp may cause corneal dystrophies, which ultimately lead to loss of vision. The majority of the disease-causing mutations are located in the C-terminal domain of TGFBIp, referred as the fourth fascilin-1 (FAS1-4) domain. In the present study the FAS1-4 Ala546Thr, a mutation that causes lattice corneal dystrophy, was investigated in dimethylsulfoxide using liquid-state NMR spectroscopy, to enable H/D exchange strategies for identification of the core formed in mature fibrils. Isotope-labeled fibrillated FAS1-4 A546T was dissolved in a ternary mixture 95/4/1 v/v/v% dimethylsulfoxide/water/trifluoroacetic acid, to obtain and assign a reference 2D (1)H-(15)N HSQC spectrum for the H/D exchange analysis. Here, we report the near-complete assignments of backbone and aliphatic side chain (1)H, (13)C and (15)N resonances for unfolded FAS1-4 A546T at 25 °C.

Keywords: Corneal dystrophy; DMSO; FAS1-4 domain; H/D-exchange NMR spectroscopy; TGFBIp.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carbon Isotopes
  • Dimethyl Sulfoxide / pharmacology*
  • Extracellular Matrix Proteins / chemistry*
  • Extracellular Matrix Proteins / metabolism*
  • Humans
  • Mutant Proteins / chemistry*
  • Mutant Proteins / metabolism*
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Denaturation / drug effects*
  • Protein Domains
  • Transforming Growth Factor beta / chemistry*
  • Transforming Growth Factor beta / metabolism*
  • Tritium


  • Carbon Isotopes
  • Extracellular Matrix Proteins
  • Mutant Proteins
  • Nitrogen Isotopes
  • Transforming Growth Factor beta
  • Tritium
  • betaIG-H3 protein
  • Dimethyl Sulfoxide