Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy.

Journal article

Oriented and unoriented M13 coat protein, incorporated into dimyristoyl phosphatidylcholine bilayers, has been studied by (13)C-magic angle spinning nuclear magnetic resonance (MAS NMR) spectroscopy. Rotational resonance experiments provided two distance constraints between Calpha and Candz.dbnd6;O positions of the labelled residues Val-29/Val-30 (0.4+/-0.5nm) and Val-29/Val-31 (0.45+/-0. 5nm) in its hydrophobic domain. The derived dihedral angles (Phi, Psi) for Val-30 revealed a local alpha-helical conformation. (13)C-CP-MAS experiments on uniformly aligned samples (MAOSS experiments) using the (13)Candz.dbnd6;O labelled site of Val-30 allowed the determination of the helix tilt (20 degrees +/-10 degrees ) in the membrane. It is shown that one uniform MAS high-resolution solid state NMR approach can be used to obtain structural and orientational data.

Authors: Glaubitz, C; Gröbner, G; Watts, A

• Publication status: Published
• Journal: Biochimica et biophysica acta
• Volume: 1463
• Issue: 1
• Pages: 151-161
• Publication date: 2000-01-01
• DOI: 10.1016/s0005-2736(99)00195-9
• ISSN: 0006-3002
• Language: English
• Keywords: Amino Acid Sequence; Molecular Sequence Data; Models, Molecular; Membrane Proteins; Bacteriophage M13; Capsid Proteins; Magnetic Resonance Spectroscopy; Protein Structure, Tertiary; Capsid