메뉴 건너뛰기




Volumn 70, Issue 4, 1996, Pages 1728-1736

Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOLAMBAN;

EID: 0029916523     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79735-7     Document Type: Article
Times cited : (76)

References (57)
  • 1
    • 0029557910 scopus 로고
    • Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban
    • Adams, P. D., I. T. Arkin, D. M. Engelman, and A. T. Brunger. 1995. Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban. Nature Struct. Biol 2:154-159.
    • (1995) Nature Struct. Biol , vol.2 , pp. 154-159
    • Adams, P.D.1    Arkin, I.T.2    Engelman, D.M.3    Brunger, A.T.4
  • 2
    • 0028063482 scopus 로고
    • Structural organization of the pentameric transmembrane α-helices of phospholamban, a cardiac ion channel
    • Arkin, I. T., P. D. Adams, K. R. MacKenzie, M. A. Lemmon, A. T. Brunger, and D. M. Engelman. 1994. Structural organization of the pentameric transmembrane α-helices of phospholamban, a cardiac ion channel. EMBO J. 13:4757-4764.
    • (1994) EMBO J. , vol.13 , pp. 4757-4764
    • Arkin, I.T.1    Adams, P.D.2    MacKenzie, K.R.3    Lemmon, M.A.4    Brunger, A.T.5    Engelman, D.M.6
  • 5
    • 0000591955 scopus 로고
    • Vibrational analysis of peptides, polypeptides, and proteins: Characteristic amide bands of β-turns
    • Bandekar, J., and S. Krimm. 1979. Vibrational analysis of peptides, polypeptides, and proteins: characteristic amide bands of β-turns. Proc. Natl. Acad. Sci. USA. 76:774-777.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 774-777
    • Bandekar, J.1    Krimm, S.2
  • 6
    • 0000325270 scopus 로고
    • The deuterium-hydrogen exchange of water-soluble polypeptides and proteins as measured by infrared spectroscopy
    • Blout, E. R., C. de Loze, and A. Asadourian. 1961. The deuterium-hydrogen exchange of water-soluble polypeptides and proteins as measured by infrared spectroscopy. J. Am. Chem. Soc. 83:1895-1900.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 1895-1900
    • Blout, E.R.1    De Loze, C.2    Asadourian, A.3
  • 8
    • 0023776215 scopus 로고
    • Fourier transform infrared techniques for probing membrane protein structure
    • Braiman, M. S., and K. J. Rothschild. 1988. Fourier transform infrared techniques for probing membrane protein structure. Annu. Rev. Biophys. Biophys. Chem. 17:541-570.
    • (1988) Annu. Rev. Biophys. Biophys. Chem. , vol.17 , pp. 541-570
    • Braiman, M.S.1    Rothschild, K.J.2
  • 9
    • 0017927954 scopus 로고
    • Neutron diffraction studies on selectively deuterated phospholipid bilayers
    • Buldt, G., H. U. Gally, A. Seelig, J. Seelig, and G. Zaccai. 1978. Neutron diffraction studies on selectively deuterated phospholipid bilayers. Nature. 271:182-184.
    • (1978) Nature , vol.271 , pp. 182-184
    • Buldt, G.1    Gally, H.U.2    Seelig, A.3    Seelig, J.4    Zaccai, G.5
  • 10
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, M. D., and H. Susi. 1986. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers. 25:469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, M.D.1    Susi, H.2
  • 11
    • 0021755229 scopus 로고
    • Polymorphic phase behaviour of phospholipid membranes studied by infrared spectroscopy
    • Casal, H. L., and H. H. Manisch 1984. Polymorphic phase behaviour of phospholipid membranes studied by infrared spectroscopy. Biochim. Biophys. Acta. 779:381-401.
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 381-401
    • Casal, H.L.1    Manisch, H.H.2
  • 12
    • 0026982657 scopus 로고
    • Fourier transform infrared analysis of bacteriorhodopsin secondary structure
    • Cladera, J., M. Sabes, and E. Padros. 1992. Fourier transform infrared analysis of bacteriorhodopsin secondary structure. Biochemistry. 31: 12363-12368.
    • (1992) Biochemistry , vol.31 , pp. 12363-12368
    • Cladera, J.1    Sabes, M.2    Padros, E.3
  • 13
    • 0018851718 scopus 로고
    • Surface-induced lamellar orientation of multilayer membrane arrays: Theoretical analysis and a new method with application to purple membrane fragments
    • Clark, N. A., K. J. Rothschild, D. A. Luippold, and A. Simon. 1980. Surface-induced lamellar orientation of multilayer membrane arrays: theoretical analysis and a new method with application to purple membrane fragments. Biophys J. 31:65-96.
    • (1980) Biophys J. , vol.31 , pp. 65-96
    • Clark, N.A.1    Rothschild, K.J.2    Luippold, D.A.3    Simon, A.4
  • 14
    • 0022968813 scopus 로고
    • Infrared spectroscopic study of photoreceptor membrane and purple membrane. Protein secondary structure and hydrogen deuterium exchange
    • Downer, N. W., T. J. Bruchman, and J. H. Hazzard. 1986. Infrared spectroscopic study of photoreceptor membrane and purple membrane. Protein secondary structure and hydrogen deuterium exchange. J. Biol. Chem. 261:3640-3647.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3640-3647
    • Downer, N.W.1    Bruchman, T.J.2    Hazzard, J.H.3
  • 15
    • 0021430848 scopus 로고
    • Vibrational analysis of peptides, polypeptides, and proteins. XVIII. Conformational sensitivity of the α-helix spectrum: αI- and αII-poly(L-alanine)
    • Dwivedi, A. M., and S. Krimm. 1984. Vibrational analysis of peptides, polypeptides, and proteins. XVIII. Conformational sensitivity of the α-helix spectrum: αI- and αII-poly(L-alanine). Biopolymers. 23: 923-924.
    • (1984) Biopolymers , vol.23 , pp. 923-924
    • Dwivedi, A.M.1    Krimm, S.2
  • 16
    • 0025608693 scopus 로고
    • Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane α helices are resistant to hydrogen/deuterium exchange
    • Earnest, T. N., J. Herzfeld, and K. J. Rothschild. 1990. Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane α helices are resistant to hydrogen/deuterium exchange. Biophys. J. 58: 1539-1546.
    • (1990) Biophys. J. , vol.58 , pp. 1539-1546
    • Earnest, T.N.1    Herzfeld, J.2    Rothschild, K.J.3
  • 18
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers
    • Frey, S., and L. K. Tamm. 1991. Orientation of melittin in phospholipid bilayers. Biophys. J. 60:922-930.
    • (1991) Biophys. J. , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 19
    • 0024451546 scopus 로고
    • Polarized infrared absorption of Na+/K+-ATPase studied by attenuated total reflection spectroscopy
    • Fringeli, U. P., H. J. Apell, M. Fringeli, P. Läuger. 1989. Polarized infrared absorption of Na+/K+-ATPase studied by attenuated total reflection spectroscopy. Biochim. Biophys. Acta. 984:301-312.
    • (1989) Biochim. Biophys. Acta , vol.984 , pp. 301-312
    • Fringeli, U.P.1    Apell, H.J.2    Fringeli, M.3    Läuger, P.4
  • 20
    • 0028709095 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds
    • H. J. Hilderson and G. B. Ralston, editors. Plenum Press, New York
    • Goormaghtigh, E., V. Cabiaux, and J-M. Ruysschaert. 1994a. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. I. Assignments and model compounds. In Subcellular Biochemistry, Vol. 23. H. J. Hilderson and G. B. Ralston, editors. Plenum Press, New York. 329-363.
    • (1994) Subcellular Biochemistry , vol.23 , pp. 329-363
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 21
    • 0028723860 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. II. Experimental aspects, side chain structure, and H/D exchange
    • H. J. Hilderson and G. B. Ralston, editors. Plenum Press, New York
    • Goormaghtigh, E., V. Cabiaux, and J-M. Ruysschaert. 1994b. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. II. Experimental aspects, side chain structure, and H/D exchange. In Subcellular Biochemistry, Vol. 23. H. J. Hilderson and G. B. Ralston, editors. Plenum Press, New York. 364-403.
    • (1994) Subcellular Biochemistry , vol.23 , pp. 364-403
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 22
    • 0028709475 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures
    • H. J. Hilderson and G. B. Ralston, editors. Plenum Press, New York
    • Goormaghtigh, E., V. Cabiaux, and J-M. Ruysschaert. 1994c. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. secondary structures. In Subcellular Biochemistry, Vol. 23. H. J. Hilderson and G. B. Ralston, editors. Plenum Press, New York. 405-450.
    • (1994) Subcellular Biochemistry , vol.23 , pp. 405-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 23
    • 0024564561 scopus 로고
    • Fourier transform infrared spectroscopic investigation of rhodopsin structure and its comparison with bacteriorhodopsin
    • Haris, P. I. M. Coke, and D. Chapman. 1989. Fourier transform infrared spectroscopic investigation of rhodopsin structure and its comparison with bacteriorhodopsin. Biochim. Biophys. Acta. 995:160-167.
    • (1989) Biochim. Biophys. Acta , vol.995 , pp. 160-167
    • Haris, P.I.1    Coke, M.2    Chapman, D.3
  • 25
    • 0024165905 scopus 로고
    • Phospholamban forms Ca-selective channels in lipid bilayers
    • Kovacs, R. J., M. T. Nelson, H. K. B. Simmerman, and L. R. Jones. 1988. Phospholamban forms Ca-selective channels in lipid bilayers. J. Biol. Chem. 263:18364-18368.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18364-18368
    • Kovacs, R.J.1    Nelson, M.T.2    Simmerman, H.K.B.3    Jones, L.R.4
  • 26
    • 0027987329 scopus 로고
    • Components of the carbonyl stretching band in the IR spectra of hydrated 1,2-diacylglycerolipid bilayers: A reevaluation
    • Lewis, R. N. A. H., R. N. McElhaney, W. Pohle, and H. H. Mantsch. 1994. Components of the carbonyl stretching band in the IR spectra of hydrated 1,2-diacylglycerolipid bilayers: a reevaluation. Biophys. J. 67: 2367-2375.
    • (1994) Biophys. J. , vol.67 , pp. 2367-2375
    • Lewis, R.N.A.H.1    McElhaney, R.N.2    Pohle, W.3    Mantsch, H.H.4
  • 27
    • 0028988375 scopus 로고
    • Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: The peptide carbonyl group of Tyr 185 is structurally active during the bR→N transition
    • Ludlam, C. F. C., S. Sonar, C-P. Lee, M. Coleman, J. Herzfeld, U. L. Rajbhandary, and K. J. Rothschild. 1995. Site-directed isotope labeling and ATR-FTIR difference spectroscopy of bacteriorhodopsin: the peptide carbonyl group of Tyr 185 is structurally active during the bR→N transition. Biochemistry. 34:2-6.
    • (1995) Biochemistry , vol.34 , pp. 2-6
    • Ludlam, C.F.C.1    Sonar, S.2    Lee, C.-P.3    Coleman, M.4    Herzfeld, J.5    Rajbhandary, U.L.6    Rothschild, K.J.7
  • 28
    • 0343629847 scopus 로고
    • Bacteriorhodopsin's M412 and BR605 protein conformations are similar. Significance for proton transport
    • Marrero, H., and K. J. Rothschild. 1987a. Bacteriorhodopsin's M412 and BR605 protein conformations are similar. Significance for proton transport. FEBS Lett. 223:289-293.
    • (1987) FEBS Lett. , vol.223 , pp. 289-293
    • Marrero, H.1    Rothschild, K.J.2
  • 29
    • 0023425518 scopus 로고
    • Conformational changes in bacteriorhodopsin studied by infrared attenuated total reflection
    • Marrero, H., and K. J. Rothschild. 1987b. Conformational changes in bacteriorhodopsin studied by infrared attenuated total reflection. Biophys. J 52:629-635.
    • (1987) Biophys. J , vol.52 , pp. 629-635
    • Marrero, H.1    Rothschild, K.J.2
  • 30
    • 0008277416 scopus 로고
    • Site specific isotopically labeled 13C vibrational difference spectroscopy gives insight into amide I′ band frequency assignments in helical peptides
    • Martinez, G. V., W. R. Fiori, and G. Millhauser. 1994. Site specific isotopically labeled 13C vibrational difference spectroscopy gives insight into amide I′ band frequency assignments in helical peptides. Biophys. J. 66:A65.
    • (1994) Biophys. J. , vol.66
    • Martinez, G.V.1    Fiori, W.R.2    Millhauser, G.3
  • 31
    • 0028361585 scopus 로고
    • Secondary structure of the nicotinic acetylcholine receptor: Implications for structural models of a ligand-gated ion channel
    • Methot, N., M. P. McCarthy, and J. E. Baenziger. 1994. Secondary structure of the nicotinic acetylcholine receptor: implications for structural models of a ligand-gated ion channel. Biochemistry. 33:7709-7717.
    • (1994) Biochemistry , vol.33 , pp. 7709-7717
    • Methot, N.1    McCarthy, M.P.2    Baenziger, J.E.3
  • 32
    • 0343532738 scopus 로고
    • The infrared spectra of polypeptides in various conformations: Amide I and amide II bands
    • Miyazawa, T., and E. R. Blout. 1961. The infrared spectra of polypeptides in various conformations: amide I and amide II bands. J. Am. Chem. Soc. 83:712-719
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 712-719
    • Miyazawa, T.1    Blout, E.R.2
  • 34
    • 0022366086 scopus 로고
    • Further characterization of protein secondary structures in purple membrane by circular dichroism and polarized infrared spectroscopies
    • Nabedryk, E., A. M. Bardin, and J. Breton. 1985. Further characterization of protein secondary structures in purple membrane by circular dichroism and polarized infrared spectroscopies. Biophys. J. 48:873-876
    • (1985) Biophys. J. , vol.48 , pp. 873-876
    • Nabedryk, E.1    Bardin, A.M.2    Breton, J.3
  • 35
    • 0019976513 scopus 로고
    • Orientation of gramicidin a transmembrane channel: Infrared dichroism study of gramicidin in vesicles
    • Nabedryk, E., M. P. Gingold, and J. Breton. 1982. Orientation of gramicidin a transmembrane channel: infrared dichroism study of gramicidin in vesicles. Biophys. J. 38:243-249.
    • (1982) Biophys. J. , vol.38 , pp. 243-249
    • Nabedryk, E.1    Gingold, M.P.2    Breton, J.3
  • 37
    • 0026025897 scopus 로고
    • Fourier transform infrared evidence for a predominantly α-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin El
    • Rath, P., O. Bousché, A. R. Merrill, W. A. Cramer, and K. J. Rothschild. 1991. Fourier transform infrared evidence for a predominantly α-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin El. Biophys. J. 59:516-522.
    • (1991) Biophys. J. , vol.59 , pp. 516-522
    • Rath, P.1    Bousché, O.2    Merrill, A.R.3    Cramer, W.A.4    Rothschild, K.J.5
  • 38
    • 0018383292 scopus 로고
    • Polarized infrared spectroscopy of oriented purple membrane
    • Rothschild, K J , and N. A. Clark. 1979. Polarized infrared spectroscopy of oriented purple membrane. Biophys. J. 25:473-488.
    • (1979) Biophys. J. , vol.25 , pp. 473-488
    • Rothschild, K.J.1    Clark, N.A.2
  • 40
    • 0018830249 scopus 로고
    • A spectroscopic study of rhodopsin α-helix orientation
    • Rothschild, K. J., R. Sanches, T. L. Hsiao, and N. A. Clark. 1980. A spectroscopic study of rhodopsin α-helix orientation. Biophys. J. 31: 53-64.
    • (1980) Biophys. J. , vol.31 , pp. 53-64
    • Rothschild, K.J.1    Sanches, R.2    Hsiao, T.L.3    Clark, N.A.4
  • 41
    • 0024415918 scopus 로고
    • Secondary structure of detergent-solubilized phospholamban, a phosphorylatable, oligometric protein of cardiac sacoplasmic reticulum
    • Simmerman, H. K. B., D. E. Lovelace, and L. R. Jones. 1989. Secondary structure of detergent-solubilized phospholamban, a phosphorylatable, oligometric protein of cardiac sacoplasmic reticulum. Biochim. Biophys. Acta. 322-329.
    • (1989) Biochim. Biophys. Acta , pp. 322-329
    • Simmerman, H.K.B.1    Lovelace, D.E.2    Jones, L.R.3
  • 44
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W., D. K. Chapman, and H. H. Mantsch. 1993. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. Biochemistry. 33:389-394.
    • (1993) Biochemistry , vol.33 , pp. 389-394
    • Surewicz, W.1    Chapman, D.K.2    Mantsch, H.H.3
  • 46
    • 0027096135 scopus 로고
    • Molecular structure and function of phospholamban in regulating the calcium pump from sarcoplasmic reticulum
    • Tada, M. 1992. Molecular structure and function of phospholamban in regulating the calcium pump from sarcoplasmic reticulum. Ann. N.Y. Acad. Sci. 671:92-102.
    • (1992) Ann. N.Y. Acad. Sci. , vol.671 , pp. 92-102
    • Tada, M.1
  • 47
    • 0024669188 scopus 로고
    • Regulation of the Ca++ pump ATPase by cAMP-dependent phosphorylation of phospholamban
    • Tada, M., and M. Kadoma. 1989. Regulation of the Ca++ pump ATPase by cAMP-dependent phosphorylation of phospholamban. BioEssays. 10:157-163.
    • (1989) BioEssays , vol.10 , pp. 157-163
    • Tada, M.1    Kadoma, M.2
  • 48
    • 0001345210 scopus 로고
    • Isotopically enhanced infrared spectroscopy: A novel method for examining secondary structure at specific sites in conformationally heterogeneous peptides
    • Tadesse, L., R. Nazarbaghi, and L. Walters. L991. Isotopically enhanced infrared spectroscopy: a novel method for examining secondary structure at specific sites in conformationally heterogeneous peptides. J. Am. Chem. Soc. 113:7036-7037.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7036-7037
    • Tadesse, L.1    Nazarbaghi, R.2    Walters, L.3
  • 49
    • 0027240319 scopus 로고
    • Orientation of functional and nonfunctional PTS permease signal sequences in lipid bilayers. A polarized attentuated total reflection infrared study
    • Tamm, L. K., and S. A. Tatulian. 1993. Orientation of functional and nonfunctional PTS permease signal sequences in lipid bilayers. A polarized attentuated total reflection infrared study. Biochemistry. 32: 7720-7726.
    • (1993) Biochemistry , vol.32 , pp. 7720-7726
    • Tamm, L.K.1    Tatulian, S.A.2
  • 50
    • 0028950657 scopus 로고
    • Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy
    • Tatulian, S. A., L. R. Jones, L. G. Reddy, D. L. Stokes, and L. K. Tamm. 1995. Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy. Biochemistry. 34:4448-4456.
    • (1995) Biochemistry , vol.34 , pp. 4448-4456
    • Tatulian, S.A.1    Jones, L.R.2    Reddy, L.G.3    Stokes, D.L.4    Tamm, L.K.5
  • 51
    • 0024294844 scopus 로고
    • Fourier transform infrared-attenuated ratal reflection spectroscopy of hydration of dimyristoylphosphatidylcholine multibilayers
    • Ter-Minassian-Saraga, L., E. Okamura, J. Umemura, and T. Takenaka. 1988. Fourier transform infrared-attenuated ratal reflection spectroscopy of hydration of dimyristoylphosphatidylcholine multibilayers. Biochim. Biophys. Acta. 946:417-423.
    • (1988) Biochim. Biophys. Acta , vol.946 , pp. 417-423
    • Ter-Minassian-Saraga, L.1    Okamura, E.2    Umemura, J.3    Takenaka, T.4
  • 52
    • 0028169263 scopus 로고
    • Amino acids Glu to Ile in the cytoplasmic domain of phospholamban are essential for functional association with the Ca-ATPase of sarcoplasmic reticulum
    • Toyofuku, T., K. Kazimierz, M. Tada, and D. H. MacLennan. 1994. Amino acids Glu to Ile in the cytoplasmic domain of phospholamban are essential for functional association with the Ca-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 269:3088-3094.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3088-3094
    • Toyofuku, T.1    Kazimierz, K.2    Tada, M.3    MacLennan, D.H.4
  • 53
    • 0001242101 scopus 로고
    • Infrared dichroism and molecular conformation of α-form poly-g-benzyl-L-glutamate
    • Tsuboi, M. 1962. Infrared dichroism and molecular conformation of α-form poly-g-benzyl-L-glutamate. J. Polym. Sci. 59:139-153.
    • (1962) J. Polym. Sci. , vol.59 , pp. 139-153
    • Tsuboi, M.1
  • 54
    • 0024360671 scopus 로고
    • Phospholamban phosphorylation in intact ventricles: Phosphorylation of serine 16 and threonine 17 in response to β-adrenergic stimulation
    • Wegener, A. D., H. K. B. Simmerman, J. P. Lindemann, and L. R. Jones. 1989. Phospholamban phosphorylation in intact ventricles: phosphorylation of serine 16 and threonine 17 in response to β-adrenergic stimulation. J Biol. Chem. 264:11468-11474.
    • (1989) J Biol. Chem. , vol.264 , pp. 11468-11474
    • Wegener, A.D.1    Simmerman, H.K.B.2    Lindemann, J.P.3    Jones, L.R.4
  • 56
    • 0026482964 scopus 로고
    • FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane α-helices of membrane proteins
    • Zhang, Y. P., R N. A. H. Lewis, R. S. Hodges, and R. N. McElhaney. 1992. FTIR spectroscopic studies of the conformation and amide hydrogen exchange of a peptide model of the hydrophobic transmembrane α-helices of membrane proteins Biochemistry. 31:11572-11578.
    • (1992) Biochemistry , vol.31 , pp. 11572-11578
    • Zhang, Y.P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4
  • 57
    • 0028950310 scopus 로고
    • Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetric and FTIR spectroscopic studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine bilayers
    • Zhang, Y-P., R. N. A. H. Lewis, R. S. Hodges, and R. N. McElhaney. 1995. Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetric and FTIR spectroscopic studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine bilayers. Biochemistry. 34:2362-2371.
    • (1995) Biochemistry , vol.34 , pp. 2362-2371
    • Zhang, Y.-P.1    Lewis, R.N.A.H.2    Hodges, R.S.3    McElhaney, R.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.