Details

Autor(en) / Beteiligte

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

Titel

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

Ist Teil von

• Biomolecular NMR assignments, 2016-04, Vol.10 (1), p.25-29

Ort / Verlag

Dordrecht: Springer Netherlands

Erscheinungsjahr

2016

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.