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Volumn 17, Issue 4, 2007, Pages 460-466

Modulating membrane protein stability and association by design

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 34548854253     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2007.08.006     Document Type: Review
Times cited : (5)

References (55)
  • 1
    • 4444247468 scopus 로고    scopus 로고
    • Functional engineered channels and pores (Review)
    • Bayley H., and Jayasinghe L. Functional engineered channels and pores (Review). Mol Membr Biol 21 (2004) 209-220
    • (2004) Mol Membr Biol , vol.21 , pp. 209-220
    • Bayley, H.1    Jayasinghe, L.2
  • 3
    • 0033135227 scopus 로고    scopus 로고
    • Computational protein design
    • Street A.G., and Mayo S.L. Computational protein design. Structure 7 (1999) R105-R109
    • (1999) Structure , vol.7
    • Street, A.G.1    Mayo, S.L.2
  • 4
    • 28444488355 scopus 로고    scopus 로고
    • Solving the membrane protein folding problem
    • Bowie J.U. Solving the membrane protein folding problem. Nature 438 (2005) 581-589
    • (2005) Nature , vol.438 , pp. 581-589
    • Bowie, J.U.1
  • 5
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: the two-stage model
    • Popot J.L., and Engelman D.M. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29 (1990) 4031-4037
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 6
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: structure and implications
    • MacKenzie K.R., Prestegard J.H., and Engelman D.M. A transmembrane helix dimer: structure and implications. Science 276 (1997) 131-133
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 7
    • 0032584233 scopus 로고    scopus 로고
    • Structure-based prediction of the stability of transmembrane helix-helix interactions: the sequence dependence of glycophorin A dimerization
    • MacKenzie K.R., and Engelman D.M. Structure-based prediction of the stability of transmembrane helix-helix interactions: the sequence dependence of glycophorin A dimerization. Proc Natl Acad Sci USA 95 (1998) 3583-3590
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3583-3590
    • MacKenzie, K.R.1    Engelman, D.M.2
  • 10
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • Choma C., Gratkowski H., Lear J.D., and DeGrado W.F. Asparagine-mediated self-association of a model transmembrane helix. Nat Struct Biol 7 (2000) 161-166
    • (2000) Nat Struct Biol , vol.7 , pp. 161-166
    • Choma, C.1    Gratkowski, H.2    Lear, J.D.3    DeGrado, W.F.4
  • 11
    • 0007949690 scopus 로고    scopus 로고
    • Interhelical hydrogen bonding drives strong interactions in membrane proteins
    • Zhou F.X., Cocco M.J., Russ W.P., Brunger A.T., and Engelman D.M. Interhelical hydrogen bonding drives strong interactions in membrane proteins. Nat Struct Biol 7 (2000) 154-160
    • (2000) Nat Struct Biol , vol.7 , pp. 154-160
    • Zhou, F.X.1    Cocco, M.J.2    Russ, W.P.3    Brunger, A.T.4    Engelman, D.M.5
  • 13
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski H., Lear J.D., and DeGrado W.F. Polar side chains drive the association of model transmembrane peptides. Proc Natl Acad Sci USA 98 (2001) 880-885
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    DeGrado, W.F.3
  • 14
    • 33645470254 scopus 로고    scopus 로고
    • Polar networks control oligomeric assembly in membranes
    • Tatko C.D., Nanda V., Lear J.D., and Degrado W.F. Polar networks control oligomeric assembly in membranes. J Am Chem Soc 128 (2006) 4170-4171
    • (2006) J Am Chem Soc , vol.128 , pp. 4170-4171
    • Tatko, C.D.1    Nanda, V.2    Lear, J.D.3    Degrado, W.F.4
  • 15
    • 0036301006 scopus 로고    scopus 로고
    • Motifs of serine and threonine can drive association of transmembrane helices
    • Dawson J.P., Weinger J.S., and Engelman D.M. Motifs of serine and threonine can drive association of transmembrane helices. J Mol Biol 316 (2002) 799-805
    • (2002) J Mol Biol , vol.316 , pp. 799-805
    • Dawson, J.P.1    Weinger, J.S.2    Engelman, D.M.3
  • 16
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: a framework for transmembrane helix-helix association
    • Russ W.P., and Engelman D.M. The GxxxG motif: a framework for transmembrane helix-helix association. J Mol Biol 296 (2000) 911-919
    • (2000) J Mol Biol , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 17
    • 0034711958 scopus 로고    scopus 로고
    • Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions
    • Senes A., Gerstein M., and Engelman D.M. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions. J Mol Biol 296 (2000) 921-936
    • (2000) J Mol Biol , vol.296 , pp. 921-936
    • Senes, A.1    Gerstein, M.2    Engelman, D.M.3
  • 18
    • 0035807810 scopus 로고    scopus 로고
    • Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants
    • Fleming K.G., and Engelman D.M. Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants. Proc Natl Acad Sci USA 98 (2001) 14340-14344
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14340-14344
    • Fleming, K.G.1    Engelman, D.M.2
  • 19
    • 5144227144 scopus 로고    scopus 로고
    • Motifs of two small residues can assist but are not sufficient to mediate transmembrane helix interactions
    • Schneider D., and Engelman D.M. Motifs of two small residues can assist but are not sufficient to mediate transmembrane helix interactions. J Mol Biol 343 (2004) 799-804
    • (2004) J Mol Biol , vol.343 , pp. 799-804
    • Schneider, D.1    Engelman, D.M.2
  • 20
    • 3843102625 scopus 로고    scopus 로고
    • Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer
    • Doura A.K., Kobus F.J., Dubrovsky L., Hibbard E., and Fleming K.G. Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer. J Mol Biol 341 (2004) 991-998
    • (2004) J Mol Biol , vol.341 , pp. 991-998
    • Doura, A.K.1    Kobus, F.J.2    Dubrovsky, L.3    Hibbard, E.4    Fleming, K.G.5
  • 21
    • 1942469334 scopus 로고    scopus 로고
    • The affinity of GXXXG motifs in transmembrane helix-helix interactions is modulated by long-range communication
    • Melnyk R.A., Kim S., Curran A.R., Engelman D.M., Bowie J.U., and Deber C.M. The affinity of GXXXG motifs in transmembrane helix-helix interactions is modulated by long-range communication. J Biol Chem 279 (2004) 16591-16597
    • (2004) J Biol Chem , vol.279 , pp. 16591-16597
    • Melnyk, R.A.1    Kim, S.2    Curran, A.R.3    Engelman, D.M.4    Bowie, J.U.5    Deber, C.M.6
  • 22
    • 33751088317 scopus 로고    scopus 로고
    • Sequence dependence of BNIP3 transmembrane domain dimerization implicates side-chain hydrogen bonding and a tandem GxxxG motif in specific helix-helix interactions
    • Results from this study show that polar substitutions away from the dimer interface can be disruptive. The authors suggest that these polar mutations stabilize an unfolded monomeric conformation not prone to optimal transmembrane helical association.
    • Sulistijo E.S., and MacKenzie K.R. Sequence dependence of BNIP3 transmembrane domain dimerization implicates side-chain hydrogen bonding and a tandem GxxxG motif in specific helix-helix interactions. J Mol Biol 364 (2006) 974-990. Results from this study show that polar substitutions away from the dimer interface can be disruptive. The authors suggest that these polar mutations stabilize an unfolded monomeric conformation not prone to optimal transmembrane helical association.
    • (2006) J Mol Biol , vol.364 , pp. 974-990
    • Sulistijo, E.S.1    MacKenzie, K.R.2
  • 23
    • 13444287923 scopus 로고    scopus 로고
    • The GxxxG-containing transmembrane domain of the CCK4 oncogene does not encode preferential self-interactions
    • Kobus F.J., and Fleming K.G. The GxxxG-containing transmembrane domain of the CCK4 oncogene does not encode preferential self-interactions. Biochemistry 44 (2005) 1464-1470
    • (2005) Biochemistry , vol.44 , pp. 1464-1470
    • Kobus, F.J.1    Fleming, K.G.2
  • 24
    • 6344236852 scopus 로고    scopus 로고
    • Complex interactions at the helix-helix interface stabilize the glycophorin A transmembrane dimer
    • Doura A.K., and Fleming K.G. Complex interactions at the helix-helix interface stabilize the glycophorin A transmembrane dimer. J Mol Biol 343 (2004) 1487-1497
    • (2004) J Mol Biol , vol.343 , pp. 1487-1497
    • Doura, A.K.1    Fleming, K.G.2
  • 25
    • 0038499536 scopus 로고    scopus 로고
    • Sequence context strongly modulates association of polar residues in transmembrane helices
    • Dawson J.P., Melnyk R.A., Deber C.M., and Engelman D.M. Sequence context strongly modulates association of polar residues in transmembrane helices. J Mol Biol 331 (2003) 255-262
    • (2003) J Mol Biol , vol.331 , pp. 255-262
    • Dawson, J.P.1    Melnyk, R.A.2    Deber, C.M.3    Engelman, D.M.4
  • 27
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • A remarkable study that measures how the amino acid composition and their position in TMH affect their translocation in biological membranes. This translocation process seems to follow simple thermodynamic rules, close to those that govern the in vitro partitioning of single peptides into organic solvents.
    • Hessa T., Kim H., Bihlmaier K., Lundin C., Boekel J., Andersson H., Nilsson I., White S.H., and von Heijne G. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433 (2005) 377-381. A remarkable study that measures how the amino acid composition and their position in TMH affect their translocation in biological membranes. This translocation process seems to follow simple thermodynamic rules, close to those that govern the in vitro partitioning of single peptides into organic solvents.
    • (2005) Nature , vol.433 , pp. 377-381
    • Hessa, T.1    Kim, H.2    Bihlmaier, K.3    Lundin, C.4    Boekel, J.5    Andersson, H.6    Nilsson, I.7    White, S.H.8    von Heijne, G.9
  • 28
    • 2342593131 scopus 로고    scopus 로고
    • Close agreement between the orientation dependence of hydrogen bonds observed in protein structures and quantum mechanical calculations
    • Morozov A.V., Kortemme T., Tsemekhman K., and Baker D. Close agreement between the orientation dependence of hydrogen bonds observed in protein structures and quantum mechanical calculations. Proc Natl Acad Sci USA 101 (2004) 6946-6951
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6946-6951
    • Morozov, A.V.1    Kortemme, T.2    Tsemekhman, K.3    Baker, D.4
  • 29
    • 33846399142 scopus 로고    scopus 로고
    • E(z), a depth-dependent potential for assessing the energies of insertion of amino acid side-chains into membranes: derivation and applications to determining the orientation of transmembrane and interfacial helices
    • Senes A., Chadi D.C., Law P.B., Walters R.F., Nanda V., and Degrado W.F. E(z), a depth-dependent potential for assessing the energies of insertion of amino acid side-chains into membranes: derivation and applications to determining the orientation of transmembrane and interfacial helices. J Mol Biol 366 (2007) 436-448
    • (2007) J Mol Biol , vol.366 , pp. 436-448
    • Senes, A.1    Chadi, D.C.2    Law, P.B.3    Walters, R.F.4    Nanda, V.5    Degrado, W.F.6
  • 30
    • 0038675609 scopus 로고    scopus 로고
    • Effective energy function for proteins in lipid membranes
    • Lazaridis T. Effective energy function for proteins in lipid membranes. Proteins 52 (2003) 176-192
    • (2003) Proteins , vol.52 , pp. 176-192
    • Lazaridis, T.1
  • 31
    • 12944289607 scopus 로고    scopus 로고
    • Implicit solvent simulations of peptide interactions with anionic lipid membranes
    • Lazaridis T. Implicit solvent simulations of peptide interactions with anionic lipid membranes. Proteins 58 (2005) 518-527
    • (2005) Proteins , vol.58 , pp. 518-527
    • Lazaridis, T.1
  • 32
    • 33745002504 scopus 로고    scopus 로고
    • Voltage-dependent energetics of alamethicin monomers in the membrane
    • Mottamal M., and Lazaridis T. Voltage-dependent energetics of alamethicin monomers in the membrane. Biophys Chem 122 (2006) 50-57
    • (2006) Biophys Chem , vol.122 , pp. 50-57
    • Mottamal, M.1    Lazaridis, T.2
  • 33
    • 0036536998 scopus 로고    scopus 로고
    • Theoretical and computational models of ion channels
    • Roux B. Theoretical and computational models of ion channels. Curr Opin Struct Biol 12 (2002) 182-189
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 182-189
    • Roux, B.1
  • 34
    • 18744403982 scopus 로고    scopus 로고
    • Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations
    • Im W., and Brooks III C.L. Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations. Proc Natl Acad Sci USA 102 (2005) 6771-6776
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 6771-6776
    • Im, W.1    Brooks III, C.L.2
  • 35
    • 17444426051 scopus 로고    scopus 로고
    • A generalized Born formalism for heterogeneous dielectric environments: application to the implicit modeling of biological membranes
    • Tanizaki S., and Feig M. A generalized Born formalism for heterogeneous dielectric environments: application to the implicit modeling of biological membranes. J Chem Phys 122 (2005) 124706
    • (2005) J Chem Phys , vol.122 , pp. 124706
    • Tanizaki, S.1    Feig, M.2
  • 36
    • 13444279948 scopus 로고    scopus 로고
    • The contribution of C alpha-H⋯O hydrogen bonds to membrane protein stability depends on the position of the amide
    • This study shows that a simple electrostatic treatment of polar interactions is sufficient to reconcile apparent contradicting experimental results concerning the contribution of weak C alpha-H⋯O hydrogen bonds to TMH stability.
    • Mottamal M., and Lazaridis T. The contribution of C alpha-H⋯O hydrogen bonds to membrane protein stability depends on the position of the amide. Biochemistry 44 (2005) 1607-1613. This study shows that a simple electrostatic treatment of polar interactions is sufficient to reconcile apparent contradicting experimental results concerning the contribution of weak C alpha-H⋯O hydrogen bonds to TMH stability.
    • (2005) Biochemistry , vol.44 , pp. 1607-1613
    • Mottamal, M.1    Lazaridis, T.2
  • 37
    • 33645096586 scopus 로고    scopus 로고
    • Transmembrane helix heterodimerization in lipid bilayers: probing the energetics behind autosomal dominant growth disorders
    • The authors present the theory and protocol to characterize the energetics of heterodimerization in lipid bilayers using FRET. They used the technique to quantify the propensity of a disease-related mutant of the TM domain of FGFR3 to heterodimerize with the wild-type domain.
    • Merzlyakov M., You M., Li E., and Hristova K. Transmembrane helix heterodimerization in lipid bilayers: probing the energetics behind autosomal dominant growth disorders. J Mol Biol 358 (2006) 1-7. The authors present the theory and protocol to characterize the energetics of heterodimerization in lipid bilayers using FRET. They used the technique to quantify the propensity of a disease-related mutant of the TM domain of FGFR3 to heterodimerize with the wild-type domain.
    • (2006) J Mol Biol , vol.358 , pp. 1-7
    • Merzlyakov, M.1    You, M.2    Li, E.3    Hristova, K.4
  • 38
    • 0345598917 scopus 로고    scopus 로고
    • Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers
    • Cristian L., Lear J.D., and DeGrado W.F. Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers. Proc Natl Acad Sci USA 100 (2003) 14772-14777
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14772-14777
    • Cristian, L.1    Lear, J.D.2    DeGrado, W.F.3
  • 39
    • 0030575833 scopus 로고    scopus 로고
    • Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator
    • Langosch D., Brosig B., Kolmar H., and Fritz H.J. Dimerisation of the glycophorin A transmembrane segment in membranes probed with the ToxR transcription activator. J Mol Biol 263 (1996) 525-530
    • (1996) J Mol Biol , vol.263 , pp. 525-530
    • Langosch, D.1    Brosig, B.2    Kolmar, H.3    Fritz, H.J.4
  • 40
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: a measure of transmembrane helix association in a biological membrane
    • Russ W.P., and Engelman D.M. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc Natl Acad Sci USA 96 (1999) 863-868
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 41
    • 0037474296 scopus 로고    scopus 로고
    • GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane
    • Schneider D., and Engelman D.M. GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane. J Biol Chem 278 (2003) 3105-3111
    • (2003) J Biol Chem , vol.278 , pp. 3105-3111
    • Schneider, D.1    Engelman, D.M.2
  • 42
    • 33646078118 scopus 로고    scopus 로고
    • The stability of transmembrane helix interactions measured in a biological membrane
    • Finger C., Volkmer T., Prodohl A., Otzen D.E., Engelman D.M., and Schneider D. The stability of transmembrane helix interactions measured in a biological membrane. J Mol Biol 358 (2006) 1221-1228
    • (2006) J Mol Biol , vol.358 , pp. 1221-1228
    • Finger, C.1    Volkmer, T.2    Prodohl, A.3    Otzen, D.E.4    Engelman, D.M.5    Schneider, D.6
  • 43
    • 0028858144 scopus 로고
    • Denaturant unfolding of the ferric enterobactin receptor and ligand-induced stabilization studied by site-directed spin labeling
    • Klug C.S., Su W., Liu J., Klebba P.E., and Feix J.B. Denaturant unfolding of the ferric enterobactin receptor and ligand-induced stabilization studied by site-directed spin labeling. Biochemistry 34 (1995) 14230-14236
    • (1995) Biochemistry , vol.34 , pp. 14230-14236
    • Klug, C.S.1    Su, W.2    Liu, J.3    Klebba, P.E.4    Feix, J.B.5
  • 44
    • 0031777549 scopus 로고    scopus 로고
    • Guanidine hydrochloride unfolding of a transmembrane beta-strand in FepA using site-directed spin labeling
    • Klug C.S., and Feix J.B. Guanidine hydrochloride unfolding of a transmembrane beta-strand in FepA using site-directed spin labeling. Protein Sci 7 (1998) 1469-1476
    • (1998) Protein Sci , vol.7 , pp. 1469-1476
    • Klug, C.S.1    Feix, J.B.2
  • 45
    • 0031010621 scopus 로고    scopus 로고
    • A method for assessing the stability of a membrane protein
    • Lau F.W., and Bowie J.U. A method for assessing the stability of a membrane protein. Biochemistry 36 (1997) 5884-5892
    • (1997) Biochemistry , vol.36 , pp. 5884-5892
    • Lau, F.W.1    Bowie, J.U.2
  • 46
    • 1642447757 scopus 로고    scopus 로고
    • Elastic coupling of integral membrane protein stability to lipid bilayer forces
    • Hong H., and Tamm L.K. Elastic coupling of integral membrane protein stability to lipid bilayer forces. Proc Natl Acad Sci USA 101 (2004) 4065-4070
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4065-4070
    • Hong, H.1    Tamm, L.K.2
  • 47
    • 33750255413 scopus 로고    scopus 로고
    • Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening
    • The first double-mutant cycle analysis to study side-chain interaction energies in a membrane protein. The authors applied a recently developed promising method [46] to measure the thermodynamic contribution of a buried electrostatic interaction network to the stability and the gating mechanism of the OmpA pore.
    • Hong H., Szabo G., and Tamm L.K. Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening. Nat Chem Biol 2 (2006) 627-635. The first double-mutant cycle analysis to study side-chain interaction energies in a membrane protein. The authors applied a recently developed promising method [46] to measure the thermodynamic contribution of a buried electrostatic interaction network to the stability and the gating mechanism of the OmpA pore.
    • (2006) Nat Chem Biol , vol.2 , pp. 627-635
    • Hong, H.1    Szabo, G.2    Tamm, L.K.3
  • 50
    • 34147130190 scopus 로고    scopus 로고
    • Computational design of peptides that target transmembrane helices
    • •] to design peptides that bind specifically to closely related integrins. Geometric complementarity to the targets was shown to be sufficient to drive binding specificity and activation of the desired integrin variants.
    • •] to design peptides that bind specifically to closely related integrins. Geometric complementarity to the targets was shown to be sufficient to drive binding specificity and activation of the desired integrin variants.
    • (2007) Science , vol.315 , pp. 1817-1822
    • Yin, H.1    Slusky, J.S.2    Berger, B.W.3    Walters, R.S.4    Vilaire, G.5    Litvinov, R.I.6    Lear, J.D.7    Caputo, G.A.8    Bennett, J.S.9    DeGrado, W.F.10
  • 52
    • 1542376209 scopus 로고    scopus 로고
    • Missense mutations in transmembrane domains of proteins: phenotypic propensity of polar residues for human disease
    • Partridge A.W., Therien A.G., and Deber C.M. Missense mutations in transmembrane domains of proteins: phenotypic propensity of polar residues for human disease. Proteins 54 (2004) 648-656
    • (2004) Proteins , vol.54 , pp. 648-656
    • Partridge, A.W.1    Therien, A.G.2    Deber, C.M.3
  • 53
    • 31344468061 scopus 로고    scopus 로고
    • FGFR3 dimer stabilization due to a single amino acid pathogenic mutation
    • Li E., You M., and Hristova K. FGFR3 dimer stabilization due to a single amino acid pathogenic mutation. J Mol Biol 356 (2006) 600-612
    • (2006) J Mol Biol , vol.356 , pp. 600-612
    • Li, E.1    You, M.2    Hristova, K.3
  • 54
    • 33751206213 scopus 로고    scopus 로고
    • Neutron diffraction studies of fluid bilayers with transmembrane proteins: structural consequences of the achondroplasia mutation
    • An interesting neutron diffraction study that shows how a polar mutation at the middle of a transmembrane spanning region can significantly affect the topology of the protein in the lipid bilayer.
    • Han X., Mihailescu M., and Hristova K. Neutron diffraction studies of fluid bilayers with transmembrane proteins: structural consequences of the achondroplasia mutation. Biophys J 91 (2006) 3736-3747. An interesting neutron diffraction study that shows how a polar mutation at the middle of a transmembrane spanning region can significantly affect the topology of the protein in the lipid bilayer.
    • (2006) Biophys J , vol.91 , pp. 3736-3747
    • Han, X.1    Mihailescu, M.2    Hristova, K.3
  • 55
    • 0035423934 scopus 로고    scopus 로고
    • Stabilizing membrane proteins
    • Bowie J.U. Stabilizing membrane proteins. Curr Opin Struct Biol 11 (2001) 397-402
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 397-402
    • Bowie, J.U.1


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