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Near-complete 1H, 13C, 15N Resonance Assignments of Dimethylsulfoxide-Denatured TGFBIp FAS1-4 A546T

Near-complete 1H, 13C, 15N Resonance Assignments of Dimethylsulfoxide-Denatured TGFBIp FAS1-4 A546T

Natalia V Kulminskaya, Yuichi Yoshimura, Kasper Runager, Charlotte S Sørensen, Morten Bjerring, Maria Andreasen, Daniel E Otzen, Jan J Enghild, Niels Chr Nielsen, Frans A A Mulder

Biomol NMR Assign. 2016 Apr;10(1):25-9.

PMID: 26275916

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42411331	Ubiquitin-13C,15N,D human			Price

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