Mechanism of interaction between the general anesthetic halothane and a model ion channel protein, II: Fluorescence and vibrational spectroscopy using a cyanophenylalanine probe.
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[1] J. Johansson,et al. Mechanism of interaction between the general anesthetic halothane and a model ion channel protein, I: Structural investigations via X-ray reflectivity from Langmuir monolayers. , 2009, Biophysical journal.
[2] J. K. Blasie,et al. Mechanism of interaction between the general anesthetic halothane and a model ion channel protein, III: Molecular dynamics simulation incorporating a cyanophenylalanine spectroscopic probe. , 2009, Biophysical journal.
[3] W. DeGrado,et al. Site-specific hydration status of an amphipathic peptide in AOT reverse micelles. , 2007, Langmuir : the ACS journal of surfaces and colloids.
[4] M. J. Tucker,et al. A novel fluorescent probe for protein binding and folding studies: p-cyano-phenylalanine. , 2006, Biopolymers.
[5] B. Johansson,et al. Diffusion and particle mobility in 1D system , 2006 .
[6] J. Johansson,et al. Monolayers of a model anesthetic-binding membrane protein: formation, characterization, and halothane-binding affinity. , 2006, Biophysical journal.
[7] M. J. Tucker,et al. Conformational distribution of a 14-residue peptide in solution: a fluorescence resonance energy transfer study. , 2005, The journal of physical chemistry. B.
[8] J. Johansson,et al. A model membrane protein for binding volatile anesthetics. , 2004, Biophysical journal.
[9] M. J. Tucker,et al. A new method for determining the local environment and orientation of individual side chains of membrane-binding peptides. , 2004, Journal of the American Chemical Society.
[10] J. Strzalka,et al. Solution to the phase problem for specular x-ray or neutron reflectivity from thin films on liquid surfaces , 2003 .
[11] S. Opella,et al. Comparative structural studies of Vpu peptides in phospholipid monolayers by x-ray scattering. , 2003, Biophysical journal.
[12] W. DeGrado,et al. Using nitrile-derivatized amino acids as infrared probes of local environment. , 2003, Journal of the American Chemical Society.
[13] R. Eckenhoff,et al. A designed four-alpha-helix bundle that binds the volatile general anesthetic halothane with high affinity. , 2000, Biophysical journal.
[14] S. Tatulian,et al. Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin. , 2000, Biochemistry.
[15] J. Reimers,et al. The Solvation of Acetonitrile , 1999 .
[16] J. Johansson,et al. A designed cavity in the hydrophobic core of a four-alpha-helix bundle improves volatile anesthetic binding affinity. , 1998, Biochemistry.
[17] R. Eckenhoff,et al. Molecular interactions between inhaled anesthetics and proteins. , 1997, Pharmacological reviews.
[18] R. L. Baldwin,et al. Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. , 1997, Biochemistry.
[19] Kiyoshi Yamamoto,et al. Complex Refractive Index Determination of Bulk Materials from Infrared Reflection Spectra , 1995 .
[20] R. Eckenhoff,et al. Binding of Halothane to Serum Albumin Demonstrated Using Tryptophan Fluorescence , 1994, Anesthesiology.
[21] W. R. Lieb,et al. Molecular and cellular mechanisms of general anaesthesia , 1994, Nature.
[22] S. Tatulian,et al. Orientation of functional and nonfunctional PTS permease signal sequences in lipid bilayers. A polarized attenuated total reflection infrared study. , 1993, Biochemistry.
[23] Gary R. Holtom,et al. Artifacts and diagnostics in fast fluorescence measurements , 1990, Photonics West - Lasers and Applications in Science and Engineering.
[24] W. Caughey,et al. Investigations of cyanide as an infrared probe of hemeprotein ligand binding sites. , 1985, The Journal of biological chemistry.
[25] Francis Crick,et al. The Fourier transform of a coiled-coil , 1953 .
[26] F. Crick,et al. The packing of α‐helices: simple coiled‐coils , 1953 .
[27] E. Goormaghtigh,et al. Attenuated total reflection IR spectroscopy as a tool to investigate the structure, orientation and tertiary structure changes in peptides and membrane proteins. , 2000, Biopolymers.