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


Journal Article

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.

Full Text

Cited Authors

  • Kulminskaya, NV; Yoshimura, Y; Runager, K; Sørensen, CS; Bjerring, M; Andreasen, M; Otzen, DE; Enghild, JJ; Nielsen, NC; Mulder, FAA

Published Date

  • April 2016

Published In

Volume / Issue

  • 10 / 1

Start / End Page

  • 25 - 29

PubMed ID

  • 26275916

Pubmed Central ID

  • 26275916

Electronic International Standard Serial Number (EISSN)

  • 1874-270X

International Standard Serial Number (ISSN)

  • 1874-2718

Digital Object Identifier (DOI)

  • 10.1007/s12104-015-9630-2


  • eng