메뉴 건너뛰기




Volumn 26, Issue 2, 1997, Pages 203-208

Stoichiometry of lipid-protein interaction and integral membrane protein structure

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0030804610     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050072     Document Type: Article
Times cited : (59)

References (58)
  • 1
    • 0030461703 scopus 로고    scopus 로고
    • Peptides modelled on the transmembrane region of the slow voltage-gated IsK potassium channel: Structural characterization of peptide assemblies in the β-strand conformation
    • Aggeli A, Boden N, Cheng YL, Findlay JBC, Knowles PF, Kovatchev P, Turnbull PJH, Horváth LI, Marsh D (1996) Peptides modelled on the transmembrane region of the slow voltage-gated IsK potassium channel: structural characterization of peptide assemblies in the β-strand conformation. Biochemistry 35:16213-16221
    • (1996) Biochemistry , vol.35 , pp. 16213-16221
    • Aggeli, A.1    Boden, N.2    Cheng, Y.L.3    Findlay, J.B.C.4    Knowles, P.F.5    Kovatchev, P.6    Turnbull, P.J.H.7    Horváth, L.I.8    Marsh, D.9
  • 2
    • 0022124340 scopus 로고
    • The uncoupling protein from brown fat mitochondria is related to the mitochondrial ADP/ATP carrier. Analysis of sequence homologies and of folding of the protein in the membrane
    • Aquila H, Link TA, Klingenberg M (1985) The uncoupling protein from brown fat mitochondria is related to the mitochondrial ADP/ATP carrier. Analysis of sequence homologies and of folding of the protein in the membrane. EMBO J 4:2369-2376
    • (1985) EMBO J , vol.4 , pp. 2369-2376
    • Aquila, H.1    Link, T.A.2    Klingenberg, M.3
  • 3
    • 0021772134 scopus 로고
    • Stoichiometry and specificity of lipid-protein interaction with myelin proteolipid protein studied by spin-label electron spin resonance
    • Brophy PJ, Horváth LI, Marsh D (1984) Stoichiometry and specificity of lipid-protein interaction with myelin proteolipid protein studied by spin-label electron spin resonance. Biochemistry 23:860-865
    • (1984) Biochemistry , vol.23 , pp. 860-865
    • Brophy, P.J.1    Horváth, L.I.2    Marsh, D.3
  • 6
    • 4244213498 scopus 로고    scopus 로고
    • Phosphorylation affects the conformation, orientation and oligomerization of phospholamban
    • Cornea RL, Autry JM, Thomas DD, Jones LR (1996) Phosphorylation affects the conformation, orientation and oligomerization of phospholamban. Biophys J 70:A256
    • (1996) Biophys J , vol.70
    • Cornea, R.L.1    Autry, J.M.2    Thomas, D.D.3    Jones, L.R.4
  • 7
    • 0021110283 scopus 로고
    • Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor
    • Ellena JF, Blazing MA, McNamee MG (1983) Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor. Biochemistry 22:5523-5535
    • (1983) Biochemistry , vol.22 , pp. 5523-5535
    • Ellena, J.F.1    Blazing, M.A.2    McNamee, M.G.3
  • 8
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman DM, Steitz TA, Goldman A (1986) Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Ann Rev Biophys Biophys Chem 15:321-353
    • (1986) Ann Rev Biophys Biophys Chem , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 9
    • 0022423909 scopus 로고
    • +)-ATPase membranes from rectal glands of Squalus acanthias
    • +)-ATPase membranes from rectal glands of Squalus acanthias. Biochemistry 24:1386-1393
    • (1985) Biochemistry , vol.24 , pp. 1386-1393
    • Esmann, M.1    Watts, A.2    Marsh, D.3
  • 11
    • 0028200088 scopus 로고
    • Structural integrity of the membrane domains in extensively trypsinized Na,K-ATPase from shark rectal glands
    • Esmann M, Karlish SJD, Sottrup-Jensen L, Marsh D (1994) Structural integrity of the membrane domains in extensively trypsinized Na,K-ATPase from shark rectal glands. Biochemistry 33:8044-8050
    • (1994) Biochemistry , vol.33 , pp. 8044-8050
    • Esmann, M.1    Karlish, S.J.D.2    Sottrup-Jensen, L.3    Marsh, D.4
  • 14
    • 0024284789 scopus 로고
    • Exchange rates at the lipid-protein interface of myelin proteolipid protein studied by spin-label electron spin resonance
    • Horváth LI, Brophy PJ, Marsh D (1988a) Exchange rates at the lipid-protein interface of myelin proteolipid protein studied by spin-label electron spin resonance. Biochemistry 27:46-52
    • (1988) Biochemistry , vol.27 , pp. 46-52
    • Horváth, L.I.1    Brophy, P.J.2    Marsh, D.3
  • 15
    • 0023785205 scopus 로고
    • Influence of lipid head-group on the specificity and exchange dynamics in lipid-protein interactions. A spin label study of myelin proteolipid apoprotein-phospholipid complexes
    • Horváth LI, Brophy PJ, Marsh D (1988b) Influence of lipid head-group on the specificity and exchange dynamics in lipid-protein interactions. A spin label study of myelin proteolipid apoprotein-phospholipid complexes. Biochemistry 27:5296-5304
    • (1988) Biochemistry , vol.27 , pp. 5296-5304
    • Horváth, L.I.1    Brophy, P.J.2    Marsh, D.3
  • 16
    • 0024533984 scopus 로고
    • Rotational diffusion of mitochondrial ADP/ATP carrier studied by saturation-transfer electron spin resonance
    • Horváth LI, Munding A, Beyer K, Klingenberg M, Marsh D (1989) Rotational diffusion of mitochondrial ADP/ATP carrier studied by saturation-transfer electron spin resonance. Biochemistry 28:407-414
    • (1989) Biochemistry , vol.28 , pp. 407-414
    • Horváth, L.I.1    Munding, A.2    Beyer, K.3    Klingenberg, M.4    Marsh, D.5
  • 17
    • 0025688183 scopus 로고
    • Lipid-protein interactions in ADP-ATP carrier/egg phosphatidylcholine recombinants studied by spin-label ESR spectroscopy
    • Horváth LI, Drees M, Beyer K, Klingenberg M, Marsh D (1990a) Lipid-protein interactions in ADP-ATP carrier/egg phosphatidylcholine recombinants studied by spin-label ESR spectroscopy. Biochemistry 29:10664-10669
    • (1990) Biochemistry , vol.29 , pp. 10664-10669
    • Horváth, L.I.1    Drees, M.2    Beyer, K.3    Klingenberg, M.4    Marsh, D.5
  • 18
    • 0025269607 scopus 로고
    • Influence of polar residue deletions on lipid-protein interactions with the myelin proteolipid protein. Spin-label ESR studies with DM-20/lipid recombinants
    • Horváth LI, Brophy PJ, Marsh D (1990b) Influence of polar residue deletions on lipid-protein interactions with the myelin proteolipid protein. Spin-label ESR studies with DM-20/lipid recombinants. Biochemistry 29:2635-2638
    • (1990) Biochemistry , vol.29 , pp. 2635-2638
    • Horváth, L.I.1    Brophy, P.J.2    Marsh, D.3
  • 19
    • 0027280812 scopus 로고
    • Exchange rates at the lipid-protein interface of the myelin proteolipid protein determined by saturation transfer electron spin resonance and continuous wave saturation studies
    • Horváth LI, Brophy PJ, Marsh D (1993) Exchange rates at the lipid-protein interface of the myelin proteolipid protein determined by saturation transfer electron spin resonance and continuous wave saturation studies. Biophys J 64:622-631
    • (1993) Biophys J , vol.64 , pp. 622-631
    • Horváth, L.I.1    Brophy, P.J.2    Marsh, D.3
  • 20
    • 0028520791 scopus 로고
    • Microwave frequency dependence of ESR spectra from spin labels undergoing two-site exchange in myelin proteolipid membranes
    • Horváth LI, Brophy PJ, Marsh D (1994) Microwave frequency dependence of ESR spectra from spin labels undergoing two-site exchange in myelin proteolipid membranes. J Magn Reson B 105:120-128
    • (1994) J Magn Reson B , vol.105 , pp. 120-128
    • Horváth, L.I.1    Brophy, P.J.2    Marsh, D.3
  • 22
    • 4243405425 scopus 로고    scopus 로고
    • Interactions of cytochrome c with reconstituted cytochrome c oxidase membranes. Evidence for increased cytochrome c oxidase boundary lipid induced by cytochrome c
    • Kleinschmidt JH, Powell GL, Marsh D (1997) Interactions of cytochrome c with reconstituted cytochrome c oxidase membranes. Evidence for increased cytochrome c oxidase boundary lipid induced by cytochrome c. Biophys J 72:A401
    • (1997) Biophys J , vol.72
    • Kleinschmidt, J.H.1    Powell, G.L.2    Marsh, D.3
  • 23
    • 0001187696 scopus 로고
    • The ADP/ATP carrier in mitochondrial membranes
    • Martonosi AN (ed) Plenum, New York
    • Klingenberg M (1985) The ADP/ATP carrier in mitochondrial membranes. In: Martonosi AN (ed) The enzymes of biological membranes, vol 4. Plenum, New York, pp 511-553
    • (1985) The Enzymes of Biological Membranes , vol.4 , pp. 511-553
    • Klingenberg, M.1
  • 24
    • 0018793910 scopus 로고
    • Spin label studies of lipid immobilization in dimyristoylphosphatidylcholine-substituted cytochrome oxidase
    • Knowles PF, Watts A, Marsh D (1979) Spin label studies of lipid immobilization in dimyristoylphosphatidylcholine-substituted cytochrome oxidase. Biochemistry 18:4480-4487
    • (1979) Biochemistry , vol.18 , pp. 4480-4487
    • Knowles, P.F.1    Watts, A.2    Marsh, D.3
  • 25
    • 0026013690 scopus 로고
    • Magnetic resonance of membranes
    • Knowles PF, Marsh D (1991) Magnetic resonance of membranes. Biochem J 274:625-641
    • (1991) Biochem J , vol.274 , pp. 625-641
    • Knowles, P.F.1    Marsh, D.2
  • 26
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 28
    • 0026538575 scopus 로고
    • Toward the molecular structure of the mitochondrial channel, VDAC
    • Mannella CA, Forte M, Columbini M (1992) Toward the molecular structure of the mitochondrial channel, VDAC. J Bioenerg Biomemb 24:7-19
    • (1992) J Bioenerg Biomemb , vol.24 , pp. 7-19
    • Mannella, C.A.1    Forte, M.2    Columbini, M.3
  • 29
    • 0000980531 scopus 로고
    • Electron spin resonance: Spin label probes
    • Metcalfe JC, Hesketh TR (eds) B426. Elsevier Amsterdam
    • Marsh D (1982) Electron spin resonance: spin label probes. In: Metcalfe JC, Hesketh TR (eds) Techniques in lipid and membrane biochemistry, vol B4/II, B426. Elsevier Amsterdam, pp 1-44
    • (1982) Techniques in Lipid and Membrane Biochemistry , vol.B4-II , pp. 1-44
    • Marsh, D.1
  • 30
    • 0041664782 scopus 로고
    • Spin label answers to lipid-protein interactions
    • Marsh D (1983) Spin label answers to lipid-protein interactions. Trends Biochem Sci 8:330-333
    • (1983) Trends Biochem Sci , vol.8 , pp. 330-333
    • Marsh, D.1
  • 31
    • 0001145625 scopus 로고
    • ESR spin label studies of lipid-protein interactions
    • Watts A, de Pont JJHHM (eds) ch 4. Elsevier, Amsterdam
    • Marsh D (1985) ESR spin label studies of lipid-protein interactions. In: Watts A, de Pont JJHHM (eds) Progress in protein-lipid interactions, vol 1, ch 4. Elsevier, Amsterdam, pp 143-172
    • (1985) Progress in Protein-lipid Interactions , vol.1 , pp. 143-172
    • Marsh, D.1
  • 32
    • 0000256168 scopus 로고
    • Experimental methods in spin-label spectral analysis
    • Berliner LJ, Reuben J (eds) Plenum, New York
    • Marsh D (1989) Experimental methods in spin-label spectral analysis. In: Berliner LJ, Reuben J (eds) Biological magnetic resonance, vol 8. Plenum, New York, pp 255-303
    • (1989) Biological Magnetic Resonance , vol.8 , pp. 255-303
    • Marsh, D.1
  • 33
    • 77956850775 scopus 로고
    • The nature of the lipid-protein interface and the influence of protein structure on protein-lipid interactions
    • Watts A (ed) Elsevier, Amsterdam
    • Marsh D (1993) The nature of the lipid-protein interface and the influence of protein structure on protein-lipid interactions. In: Watts A (ed) New comprehensive biochemistry, vol 25, Protein-lipid interactions. Elsevier, Amsterdam, pp 41-66
    • (1993) New Comprehensive Biochemistry, Vol 25, Protein-lipid Interactions , vol.25 , pp. 41-66
    • Marsh, D.1
  • 34
    • 0029870676 scopus 로고    scopus 로고
    • Peptide models for membrane channels
    • Marsh D (1996) Peptide models for membrane channels. Biochem J 315:345-361
    • (1996) Biochem J , vol.315 , pp. 345-361
    • Marsh, D.1
  • 35
    • 0030928208 scopus 로고    scopus 로고
    • Dichroic ratios in polarized FTIR for non-axial symmetry of β-sheet structures
    • in press
    • Marsh D (1997) Dichroic ratios in polarized FTIR for non-axial symmetry of β-sheet structures. Biophys J 72 (in press)
    • (1997) Biophys J , vol.72
    • Marsh, D.1
  • 36
    • 0002930379 scopus 로고
    • Spin-label studies of the structure and dynamics of lipids and proteins in membranes
    • Hoff AJ (ed) Elsevier, Amsterdam
    • Marsh D, Horváth LI (1989) Spin-label studies of the structure and dynamics of lipids and proteins in membranes. In: Hoff AJ (ed) Advanced EPR. Applications in biology and biochemistry. Elsevier, Amsterdam, pp 707-752
    • (1989) Advanced EPR. Applications in Biology and Biochemistry , pp. 707-752
    • Marsh, D.1    Horváth, L.I.2
  • 37
    • 0002316753 scopus 로고
    • Spin-labeling and lipid-protein interactions in membranes
    • Jost PC, Griffith OH (eds) Wiley-Interscience, New York
    • Marsh D, Watts A (1982) Spin-labeling and lipid-protein interactions in membranes. In: Jost PC, Griffith OH (eds) Lipid-protein interactions, vol 2. Wiley-Interscience, New York, pp 53-126
    • (1982) Lipid-protein Interactions , vol.2 , pp. 53-126
    • Marsh, D.1    Watts, A.2
  • 38
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Møller JV, Juul B, le Maire, M (1996) Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim Biophys Acta 1286:1-51
    • (1996) Biochim Biophys Acta , vol.1286 , pp. 1-51
    • Møller, J.V.1    Juul, B.2    Le Maire, M.3
  • 39
    • 0030220255 scopus 로고    scopus 로고
    • Protein folds in channel structure
    • Montai M (1996) Protein folds in channel structure. Curr Opin Struct Biol 6:499-510
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 499-510
    • Montai, M.1
  • 40
    • 0029081430 scopus 로고
    • Lipid-protein interactions and assembly of the 16-kDa channel polypeptide from Nephrops norvegicus. Studies with spin-label electron spin resonance spectroscopy and electron microscopy
    • Páli T, Finbow ME, Holzenburg A, Findlay JBC, Marsh D (1995) Lipid-protein interactions and assembly of the 16-kDa channel polypeptide from Nephrops norvegicus. Studies with spin-label electron spin resonance spectroscopy and electron microscopy. Biochemistry 34:9211-9218
    • (1995) Biochemistry , vol.34 , pp. 9211-9218
    • Páli, T.1    Finbow, M.E.2    Holzenburg, A.3    Findlay, J.B.C.4    Marsh, D.5
  • 41
    • 0023096158 scopus 로고
    • Lipid mobility and order in bovine rod outer segment disk membranes. A spin-label study of lipid-protein interactions
    • Pates RD, Marsh D (1987) Lipid mobility and order in bovine rod outer segment disk membranes. A spin-label study of lipid-protein interactions. Biochemistry 26:29-39
    • (1987) Biochemistry , vol.26 , pp. 29-39
    • Pates, R.D.1    Marsh, D.2
  • 42
    • 0021966175 scopus 로고
    • Lipid-protein interactions in frog rod outer segment disc membranes. Characterization by spin labels
    • Pates RD, Watts A, Uhl R, Marsh D (1985) Lipid-protein interactions in frog rod outer segment disc membranes. Characterization by spin labels. Biochim Biophys Acta 814:389-397
    • (1985) Biochim Biophys Acta , vol.814 , pp. 389-397
    • Pates, R.D.1    Watts, A.2    Uhl, R.3    Marsh, D.4
  • 43
    • 0026532061 scopus 로고
    • Stoichiometry, selectivity, and exchange dynamics of lipid-protein interaction with bacteriophage M13 coat protein studied by spin label electron spin resonance. Effects of protein secondary structure
    • Peelen SJCJ, Sanders JC, Hemminga MA, Marsh D (1992) Stoichiometry, selectivity, and exchange dynamics of lipid-protein interaction with bacteriophage M13 coat protein studied by spin label electron spin resonance. Effects of protein secondary structure. Biochemistry 31:2670-2677
    • (1992) Biochemistry , vol.31 , pp. 2670-2677
    • Peelen, S.J.C.J.1    Sanders, J.C.2    Hemminga, M.A.3    Marsh, D.4
  • 44
    • 0023261331 scopus 로고
    • Molecular exchange at the lipid-rhodopsin interface: Spin-label electron spin resonance studies of rhodopsin-dimyristoyl phosphatidylcholine recombinants
    • Ryba NJP, Horváth LI, Watts A, Marsh D (1987) Molecular exchange at the lipid-rhodopsin interface: spin-label electron spin resonance studies of rhodopsin-dimyristoyl phosphatidylcholine recombinants. Biochemistry 26:3234-3240
    • (1987) Biochemistry , vol.26 , pp. 3234-3240
    • Ryba, N.J.P.1    Horváth, L.I.2    Watts, A.3    Marsh, D.4
  • 45
    • 0026795003 scopus 로고
    • Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation transfer electron spin resonance
    • Ryba NJP, Marsh D (1992) Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation transfer electron spin resonance. Biochemistry 31:7511-7518
    • (1992) Biochemistry , vol.31 , pp. 7511-7518
    • Ryba, N.J.P.1    Marsh, D.2
  • 46
    • 0025800503 scopus 로고
    • Lipid-protein and protein-protein interactions in double recombinants of myelin proteolipid apoprotein and myelin basic protein with dimyristoyl-phosphatidylglycerol
    • Sankaram MB, Brophy PJ, Marsh D (1991) Lipid-protein and protein-protein interactions in double recombinants of myelin proteolipid apoprotein and myelin basic protein with dimyristoyl-phosphatidylglycerol. Biochemistry 30:5866-5873
    • (1991) Biochemistry , vol.30 , pp. 5866-5873
    • Sankaram, M.B.1    Brophy, P.J.2    Marsh, D.3
  • 47
    • 77957033404 scopus 로고
    • Principles of membrane protein structure
    • Lee AG (ed) JAI Press, Greenwich, CT
    • Sansom MSP, Kerr ID (1995) Principles of membrane protein structure. In: Lee AG (ed) Biomembranes, vol 1, JAI Press, Greenwich, CT, pp 29-78
    • (1995) Biomembranes , vol.1 , pp. 29-78
    • Sansom, M.S.P.1    Kerr, I.D.2
  • 48
    • 0029556994 scopus 로고
    • Projection structure of frog rhodopsin in two crystal forms
    • Schertler GFX, Margrave PA (1995) Projection structure of frog rhodopsin in two crystal forms. Proc Natl Acad Sci USA 92: 11578-11582
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11578-11582
    • Schertler, G.F.X.1    Margrave, P.A.2
  • 50
    • 0021359687 scopus 로고
    • Structure of the proteolipid protein extracted from bovine central nervous system myelin with nondenaturing detergents
    • Smith R, Cook J, Dickens PA (1984) Structure of the proteolipid protein extracted from bovine central nervous system myelin with nondenaturing detergents. J Neurochem 42:306-313
    • (1984) J Neurochem , vol.42 , pp. 306-313
    • Smith, R.1    Cook, J.2    Dickens, P.A.3
  • 51
    • 0020012239 scopus 로고
    • Rotational dynamics of protein and boundary lipid in sarcoplasmic reticulum membrane
    • Thomas DD, Bigelow DJ, Squier TC, Hidalgo CH (1982) Rotational dynamics of protein and boundary lipid in sarcoplasmic reticulum membrane. Biophys J 37:217-225
    • (1982) Biophys J , vol.37 , pp. 217-225
    • Thomas, D.D.1    Bigelow, D.J.2    Squier, T.C.3    Hidalgo, C.H.4
  • 53
    • 0027506299 scopus 로고
    • Nicotinic acetylcholine receptor at 9 Å resolution
    • Unwin N (1993) Nicotinic acetylcholine receptor at 9 Å resolution. J Mol Biol 229:1101-1124
    • (1993) J Mol Biol , vol.229 , pp. 1101-1124
    • Unwin, N.1
  • 54
    • 0025989688 scopus 로고
    • Do helices in membranes prefer to form bundles or stay dispersed in the lipid phase?
    • Wang J, Pullman A (1991) Do helices in membranes prefer to form bundles or stay dispersed in the lipid phase? Biochim Biophys Acta 1070:493-496
    • (1991) Biochim Biophys Acta , vol.1070 , pp. 493-496
    • Wang, J.1    Pullman, A.2
  • 55
    • 0018594495 scopus 로고
    • Rhodopsin-lipid associations in bovine rod outer segment membranes. Identification of immobilized lipid by spin labels
    • Watts A, Volotovski ID, Marsh D (1979) Rhodopsin-lipid associations in bovine rod outer segment membranes. Identification of immobilized lipid by spin labels. Biochemistry 18:5006-5013
    • (1979) Biochemistry , vol.18 , pp. 5006-5013
    • Watts, A.1    Volotovski, I.D.2    Marsh, D.3
  • 56
    • 0026980191 scopus 로고
    • Proteolipid protein (PLP) of CNS myelin: Positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP
    • Weimbs T, Stoffel W (1992) Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP. Biochemistry 31:12289-12296
    • (1992) Biochemistry , vol.31 , pp. 12289-12296
    • Weimbs, T.1    Stoffel, W.2
  • 57
    • 0024809019 scopus 로고
    • Spin-label ESR of bacteriophage M13 coat protein in mixed lipid bilayers. Characterization of molecular selectivity of charged phospholipids for the bacteriophage coat protein in lipid bilayers
    • Wolfs CJAM, Horváth LI, Marsh D, Watts A, Hemminga MA (1989) Spin-label ESR of bacteriophage M13 coat protein in mixed lipid bilayers. Characterization of molecular selectivity of charged phospholipids for the bacteriophage coat protein in lipid bilayers. Biochemistry 28:9995-10001
    • (1989) Biochemistry , vol.28 , pp. 9995-10001
    • Wolfs, C.J.A.M.1    Horváth, L.I.2    Marsh, D.3    Watts, A.4    Hemminga, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.