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By edited by Graham A. Webb.

ISBN-10: 0128003278

ISBN-13: 9780128003275

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Acta 1808 (2011) 1957–1974. N. Du¨rr, M. Gildenberg, A. Ramamoorthy, The magic of bicelles lights up membrane protein structure, Chem. Rev. 112 (2012) 6054–6074. S. Ahuja, N. -C. Im, S. Vivekanandan, N. V. Le Clair, R. Huang, R. Soong, J. Xu, K. P. Nanga, A. Bridges, L. Waskell, A. Ramamoorthy, A model of the membrane-bound cytochrome-bound b5-cytochrome P450 complex from NMR and mutagenesis data, J. Biol. Chem. 288 (2013) 22080–22095. A. R. J. P. Kirkpatrick, D. Nietlispach, Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy, Nat.

Tuzi, K. Yonebayashi, A. Naito, R. K. Lanyi, H. Saitoˆ, Surface dynamics of bacteriorhodopsin as revealed by 13C NMR studies on [13C]Ala-labeled proteins: determination of millisecond or microsecond motions in interhelical loops and C-terminal α-helix, J. Biochem. 129 (2001) 373–382. [53] S. Tuzi, A. Naito, H. Saitoˆ, 13C NMR study on conformation and dynamics of the transmembrane α-helices, loops and C-terminus of [3-13C]-Ala-labelled bacteriorhodopsin, Biochemistry 33 (1994) 15046–15052. [54] S.

31 (1997) 63–105. E. Woessner, Spin relaxation processes in a two-proton system undergoing anisotropic reorientation, J. Chem. Phys. 36 (1962) 1–4. [35] R. Richarz, K. Nagayama, K. Wu¨thrich, Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analog, Biochemistry 19 (1980) 5189–5196. W. Peng, G. Wagner, Mapping of spectral density functions using heteronuclear NMR relaxation measurements, J.

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Annual Reports on NMR Spectroscopy by edited by Graham A. Webb.

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