PDBsum entry 1av1

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Lipid transport PDB id
Protein chains
201 a.a. *
* Residue conservation analysis
PDB id:
Name: Lipid transport
Title: Crystal structure of human apolipoprotein a-i
Structure: Apolipoprotein a-i. Chain: a, b, c, d. Fragment: lipid-binding domain. Synonym: apo a-i. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: bl21. Tissue: blood. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Tetramer (from PQS)
4.00Å     R-factor:   0.382     R-free:   0.428
Authors: D.W.Borhani,D.P.Rogers,J.A.Engler,C.G.Brouillette
Key ref:
D.W.Borhani et al. (1997). Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc Natl Acad Sci U S A, 94, 12291-12296. PubMed id: 9356442 DOI: 10.1073/pnas.94.23.12291
23-Sep-97     Release date:   04-Feb-98    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P02647  (APOA1_HUMAN) -  Apolipoprotein A-I
267 a.a.
201 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     lipid transport   2 terms 
  Biochemical function     lipid binding     1 term  


DOI no: 10.1073/pnas.94.23.12291 Proc Natl Acad Sci U S A 94:12291-12296 (1997)
PubMed id: 9356442  
Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation.
D.W.Borhani, D.P.Rogers, J.A.Engler, C.G.Brouillette.
The structure of truncated human apolipoprotein A-I (apo A-I), the major protein component of high density lipoprotein, has been determined at 4-A resolution. The crystals comprise residues 44-243 (exon 4) of apo A-I, a fragment that binds to lipid similarly to intact apo A-I and that retains the lipid-bound conformation even in the absence of lipid. The molecule consists almost entirely of a pseudo-continuous, amphipathic alpha-helix that is punctuated by kinks at regularly spaced proline residues; it adopts a shape similar to a horseshoe of dimensions 125 x 80 x 40 A. Four molecules in the asymmetric unit associate via their hydrophobic faces to form an antiparallel four-helix bundle with an elliptical ring shape. Based on this structure, we propose a model for the structure of apo A-I bound to high density lipoprotein.
  Selected figure(s)  
Figure 2.
Fig. 2. Stereoviews of the apo (1-43)A-I C^ trace. (a) The apo (1-43)A-I monomer, molecule A. The N- and C-termini are labeled, as are each of the secondary structural elements described in the^ text. These elements are also colored differently. (b and c) The^ apo (1-43)A-I A/B dimer, and the tetramer. The molecules are^ colored as in a to facilitate identification of the alignment of the extensive intermolecular interactions.
Figure 4.
Fig. 4. RIBBONS (34) representation illustrating the elliptical and curved shape of the apo (1-43)A-I tetramer. (a) The tetramer is shown with the three noncrystallographic (pseudo)dyads: molecule^ A is gold, molecule B is purple, molecule C is pink, and molecule^ D is green. (b) View down the A/C dyad. (c) As in b, rotated 90° around the horizontal axis i.e., viewed down the A/D pseudo-dyad. (d) As in c, rotated 70° around the vertical axis.
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21499241 J.Frauenfeld, J.Gumbart, E.O.Sluis, S.Funes, M.Gartmann, B.Beatrix, T.Mielke, O.Berninghausen, T.Becker, K.Schulten, and R.Beckmann (2011).
Cryo-EM structure of the ribosome-SecYE complex in the membrane environment.
  Nat Struct Mol Biol, 18, 614-621.
PDB codes: 3j00 3j01
21399642 R.Huang, R.A.Silva, W.G.Jerome, A.Kontush, M.J.Chapman, L.K.Curtiss, T.J.Hodges, and W.S.Davidson (2011).
Apolipoprotein A-I structural organization in high-density lipoproteins isolated from human plasma.
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20043647 B.Shao, M.N.Oda, J.F.Oram, and J.W.Heinecke (2010).
Myeloperoxidase: an oxidative pathway for generating dysfunctional high-density lipoprotein.
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21060857 T.Vuorela, A.Catte, P.S.Niemelä, A.Hall, M.T.Hyvönen, S.J.Marrink, M.Karttunen, and I.Vattulainen (2010).
Role of lipids in spheroidal high density lipoproteins.
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19770066 V.Narayanaswami, R.S.Kiss, and P.M.Weers (2010).
The helix bundle: a reversible lipid binding motif.
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19546861 Y.Levin, L.Wang, E.Schwarz, D.Koethe, F.M.Leweke, and S.Bahn (2010).
Global proteomic profiling reveals altered proteomic signature in schizophrenia serum.
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19130896 A.C.Paula-Lima, M.A.Tricerri, J.Brito-Moreira, T.R.Bomfim, F.F.Oliveira, M.H.Magdesian, L.T.Grinberg, R.Panizzutti, and S.T.Ferreira (2009).
Human apolipoprotein A-I binds amyloid-beta and prevents Abeta-induced neurotoxicity.
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19318685 E.T.Alexander, M.Tanaka, M.Kono, H.Saito, D.J.Rader, and M.C.Phillips (2009).
Structural and functional consequences of the Milano mutation (R173C) in human apolipoprotein A-I.
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The nanodisc: a novel tool for membrane protein studies.
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Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.
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19167289 M.K.Jones, A.Catte, J.C.Patterson, F.Gu, J.Chen, L.Li, and J.P.Segrest (2009).
Thermal stability of apolipoprotein A-I in high-density lipoproteins by molecular dynamics.
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19860440 M.K.Jones, A.Catte, L.Li, and J.P.Segrest (2009).
Dynamics of activation of lecithin:cholesterol acyltransferase by apolipoprotein A-I.
  Biochemistry, 48, 11196-11210.  
19812036 Z.Wu, V.Gogonea, X.Lee, M.A.Wagner, X.M.Li, Y.Huang, A.Undurti, R.P.May, M.Haertlein, M.Moulin, I.Gutsche, G.Zaccai, J.A.Didonato, and S.L.Hazen (2009).
Double superhelix model of high density lipoprotein.
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PDB code: 3k2s
18065479 A.Catte, J.C.Patterson, D.Bashtovyy, M.K.Jones, F.Gu, L.Li, A.Rampioni, D.Sengupta, T.Vuorela, P.Niemelä, M.Karttunen, S.J.Marrink, I.Vattulainen, and J.P.Segrest (2008).
Structure of spheroidal HDL particles revealed by combined atomistic and coarse-grained simulations.
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18706282 C.R.White, G.Datta, Z.Zhang, H.Gupta, D.W.Garber, V.K.Mishra, M.N.Palgunachari, S.P.Handattu, M.Chaddha, and G.M.Anantharamaiah (2008).
HDL therapy for cardiovascular diseases: the road to HDL mimetics.
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18783334 L.Cigliano, L.D.D'Andrea, B.Maresca, M.Serino, A.Carlucci, A.Salvatore, M.S.Spagnuolo, G.Scigliuolo, C.Pedone, and P.Abrescia (2008).
Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin.
  Biol Chem, 389, 1421-1426.  
18515783 M.J.Thomas, S.Bhat, and M.G.Sorci-Thomas (2008).
Three-dimensional models of HDL apoA-I: implications for its assembly and function.
  J Lipid Res, 49, 1875-1883.  
18719128 R.A.Silva, R.Huang, J.Morris, J.Fang, E.O.Gracheva, G.Ren, A.Kontush, W.G.Jerome, K.A.Rye, and W.S.Davidson (2008).
Structure of apolipoprotein A-I in spherical high density lipoproteins of different sizes.
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18385132 R.Carnemolla, X.Ren, T.K.Biswas, S.C.Meredith, C.A.Reardon, J.Wang, and G.S.Getz (2008).
The specific amino acid sequence between helices 7 and 8 influences the binding specificity of human apolipoprotein A-I for high density lipoprotein (HDL) subclasses: a potential for HDL preferential generation.
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17993480 V.M.Bolanos-Garcia, A.Renault, and S.Beaufils (2008).
Surface rheology and adsorption kinetics reveal the relative amphiphilicity, interfacial activity, and stability of human exchangeable apolipoproteins.
  Biophys J, 94, 1735-1745.  
17447731 A.Chroni, G.Koukos, A.Duka, and V.I.Zannis (2007).
The carboxy-terminal region of apoA-I is required for the ABCA1-dependent formation of alpha-HDL but not prebeta-HDL particles in vivo.
  Biochemistry, 46, 5697-5708.  
17154396 C.Beaufils, C.Alexopoulos, M.P.Petraki, A.D.Tselepis, N.Coudevylle, M.Sakarellos-Daitsiotis, C.Sakarellos, and M.T.Cung (2007).
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17239472 I.Kratzer, K.Wernig, U.Panzenboeck, E.Bernhart, H.Reicher, R.Wronski, M.Windisch, A.Hammer, E.Malle, A.Zimmer, and W.Sattler (2007).
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17554795 M.D.Benson, and J.C.Kincaid (2007).
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17563120 S.Bhat, M.G.Sorci-Thomas, R.Tuladhar, M.P.Samuel, and M.J.Thomas (2007).
Conformational adaptation of apolipoprotein A-I to discretely sized phospholipid complexes.
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17676061 Z.Wu, M.A.Wagner, L.Zheng, J.S.Parks, J.M.Shy, J.D.Smith, V.Gogonea, and S.L.Hazen (2007).
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16452169 A.A.Ajees, G.M.Anantharamaiah, V.K.Mishra, M.M.Hussain, and H.M.Murthy (2006).
Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases.
  Proc Natl Acad Sci U S A, 103, 2126-2131.
PDB code: 2a01
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16820298 D.M.Hatters, C.A.Peters-Libeu, and K.H.Weisgraber (2006).
Apolipoprotein E structure: insights into function.
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16326917 E.Gross, D.Q.Peng, S.L.Hazen, and J.D.Smith (2006).
A novel folding intermediate state for apolipoprotein A-I: role of the amino and carboxy termini.
  Biophys J, 90, 1362-1370.  
16430220 I.N.Gorshkova, T.Liu, H.Y.Kan, A.Chroni, V.I.Zannis, and D.Atkinson (2006).
Structure and stability of apolipoprotein a-I in solution and in discoidal high-density lipoprotein probed by double charge ablation and deletion mutation.
  Biochemistry, 45, 1242-1254.  
17107880 L.Obici, G.Franceschini, L.Calabresi, S.Giorgetti, M.Stoppini, G.Merlini, and V.Bellotti (2006).
Structure, function and amyloidogenic propensity of apolipoprotein A-I.
  Amyloid, 13, 191-205.  
16680024 M.J.Thomas, S.Bhat, and M.G.Sorci-Thomas (2006).
The use of chemical cross-linking and mass spectrometry to elucidate the tertiary conformation of lipid-bound apolipoprotein A-I.
  Curr Opin Lipidol, 17, 214-220.  
16905105 N.Furnham, A.S.Doré, D.Y.Chirgadze, Bakker, M.A.Depristo, and T.L.Blundell (2006).
Knowledge-based real-space explorations for low-resolution structure determination.
  Structure, 14, 1313-1320.  
16501936 V.I.Zannis, A.Chroni, and M.Krieger (2006).
Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL.
  J Mol Med, 84, 276-294.  
16905610 Y.Li, A.Z.Kijac, S.G.Sligar, and C.M.Rienstra (2006).
Structural analysis of nanoscale self-assembled discoidal lipid bilayers by solid-state NMR spectroscopy.
  Biophys J, 91, 3819-3828.  
15533924 A.Y.Shih, I.G.Denisov, J.C.Phillips, S.G.Sligar, and K.Schulten (2005).
Molecular dynamics simulations of discoidal bilayers assembled from truncated human lipoproteins.
  Biophys J, 88, 548-556.  
16852976 I.G.Denisov, M.A.McLean, A.W.Shaw, Y.V.Grinkova, and S.G.Sligar (2005).
Thermotropic phase transition in soluble nanoscale lipid bilayers.
  J Phys Chem B, 109, 15580-15588.  
15891389 O.Gursky (2005).
Apolipoprotein structure and dynamics.
  Curr Opin Lipidol, 16, 287-294.  
15891390 W.S.Davidson, and R.A.Silva (2005).
Apolipoprotein structural organization in high density lipoproteins: belts, bundles, hinges and hairpins.
  Curr Opin Lipidol, 16, 295-300.  
15558533 C.L.Murphy, S.Wang, K.Weaver, M.A.Gertz, D.T.Weiss, and A.Solomon (2004).
Renal apolipoprotein A-I amyloidosis associated with a novel mutant Leu64Pro.
  Am J Kidney Dis, 44, 1103-1109.  
15272303 E.Papagrigoriou, A.R.Gingras, I.L.Barsukov, N.Bate, I.J.Fillingham, B.Patel, R.Frank, W.H.Ziegler, G.C.Roberts, D.R.Critchley, and J.Emsley (2004).
Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle.
  EMBO J, 23, 2942-2951.
PDB codes: 1sj7 1sj8 1t01
15678758 F.J.Stevens (2004).
Amyloid formation: an emulation of matrix protein assembly?
  Amyloid, 11, 232-244.  
15234552 H.Saito, S.Lund-Katz, and M.C.Phillips (2004).
Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins.
  Prog Lipid Res, 43, 350-380.  
15333941 L.R.Alves, P.L.Oliveira, J.A.Barbosa, B.G.Guimarães, and F.J.Medrano (2004).
Crystallization and preliminary X-ray diffraction analysis of HeLp, a heme lipoprotein from the hemolymph of the cattle tick Boophilus microplus.
  Acta Crystallogr D Biol Crystallogr, 60, 1639-1640.  
15098021 M.Harel, A.Aharoni, L.Gaidukov, B.Brumshtein, O.Khersonsky, R.Meged, H.Dvir, R.B.Ravelli, A.McCarthy, L.Toker, I.Silman, J.L.Sussman, and D.S.Tawfik (2004).
Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes.
  Nat Struct Mol Biol, 11, 412-419.
PDB code: 1v04
12819519 C.Alonso-Villaverde, T.Segues, B.Coll-Crespo, R.Pérez-Bernalte, A.Rabassa, M.Gomila, S.Parra, M.A.Gozález-Esteban, M.J.Jiménez-Expósito, and L.Masana (2003).
High-density lipoprotein concentrations relate to the clinical course of HIV viral load in patients undergoing antiretroviral therapy.
  AIDS, 17, 1173-1178.  
  14986480 D.Coriu, A.Dispenzieri, F.J.Stevens, C.L.Murphy, S.Wang, D.T.Weiss, and A.Solomon (2003).
Hepatic amyloidosis resulting from deposition of the apolipoprotein A-I variant Leu75Pro.
  Amyloid, 10, 215-223.  
12754494 M.N.Oda, T.M.Forte, R.O.Ryan, and J.C.Voss (2003).
The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger.
  Nat Struct Biol, 10, 455-460.  
12642783 Y.L.Marcel, and R.S.Kiss (2003).
Structure-function relationships of apolipoprotein A-I: a flexible protein with dynamic lipid associations.
  Curr Opin Lipidol, 14, 151-157.  
11818551 J.Wang, B.D.Sykes, and R.O.Ryan (2002).
Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein.
  Proc Natl Acad Sci U S A, 99, 1188-1193.
PDB code: 1eq1
11988467 R.J.Cushley, and M.Okon (2002).
NMR studies of lipoprotein structure.
  Annu Rev Biophys Biomol Struct, 31, 177-206.  
11959505 S.Pokutta, and W.I.Weis (2002).
The cytoplasmic face of cell contact sites.
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11278170 C.G.Brouillette, G.M.Anantharamaiah, J.A.Engler, and D.W.Borhani (2001).
Structural models of human apolipoprotein A-I: a critical analysis and review.
  Biochim Biophys Acta, 1531, 4.  
11266606 P.Mangione, M.Sunde, S.Giorgetti, M.Stoppini, G.Esposito, L.Gianelli, L.Obici, L.Asti, A.Andreola, P.Viglino, G.Merlini, and V.Bellotti (2001).
Amyloid fibrils derived from the apolipoprotein A1 Leu174Ser variant contain elements of ordered helical structure.
  Protein Sci, 10, 187-199.  
11325616 R.S.Kiss, R.O.Ryan, and G.A.Francis (2001).
Functional similarities of human and chicken apolipoprotein A-I: dependence on secondary and tertiary rather than primary structure.
  Biochim Biophys Acta, 1531, 251-259.  
10969027 A.E.Klon, M.K.Jones, J.P.Segrest, and S.C.Harvey (2000).
Molecular belt models for the apolipoprotein A-I Paris and Milano mutations.
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Pyrene excimer fluorescence: a spatially sensitive probe to monitor lipid-induced helical rearrangement of apolipophorin III.
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10787171 J.P.Segrest, L.Li, G.M.Anantharamaiah, S.C.Harvey, K.N.Liadaki, and V.Zannis (2000).
Structure and function of apolipoprotein A-I and high-density lipoprotein.
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11087425 M.A.Tricerri, A.K.Behling Agree, S.A.Sanchez, and A.Jonas (2000).
Characterization of apolipoprotein A-I structure using a cysteine-specific fluorescence probe.
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Apolipoprotein AI and transthyretin as components of amyloid fibrils in a kindred with apoAI Leu178His amyloidosis.
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Lipid binding of the exchangeable apolipoprotein apolipophorin III induces major changes in fluorescence properties of tryptophans 115 and 130.
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Molecular basis of exchangeable apolipoprotein function.
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Molecular dynamics on a model for nascent high-density lipoprotein: role of salt bridges.
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Effect of apolipoprotein A-I lipidation on the formation and function of pre-beta and alpha-migrating LpA-I particles.
  Biochemistry, 38, 1727-1735.  
10489452 D.W.Borhani, J.A.Engler, and C.G.Brouillette (1999).
Crystallization of truncated human apolipoprotein A-I in a novel conformation.
  Acta Crystallogr D Biol Crystallogr, 55, 1578-1583.  
10666577 D.W.Borhani, J.A.Engler, and C.G.Brouillette (1999).
Human apolipoprotein A-I: structure determination and analysis of unusual diffraction characteristics.
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The new apolipoprotein A-I variant leu(174) --> Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide.
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  10548051 O.Gursky (1999).
Probing the conformation of a human apolipoprotein C-1 by amino acid substitutions and trimethylamine-N-oxide.
  Protein Sci, 8, 2055-2064.  
10194351 R.S.Kiss, C.M.Kay, and R.O.Ryan (1999).
Amphipathic alpha-helix bundle organization of lipid-free chicken apolipoprotein A-I.
  Biochemistry, 38, 4327-4334.  
10357827 T.Ahola, A.Lampio, P.Auvinen, and L.Kääriäinen (1999).
Semliki Forest virus mRNA capping enzyme requires association with anionic membrane phospholipids for activity.
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10572013 W.S.Davidson, K.Arnvig-McGuire, A.Kennedy, J.Kosman, T.L.Hazlett, and A.Jonas (1999).
Structural organization of the N-terminal domain of apolipoprotein A-I: studies of tryptophan mutants.
  Biochemistry, 38, 14387-14395.  
10089535 A.Saxena, A.Gries, R.Schwarzenbacher, G.M.Kostner, P.Laggner, and R.Prassl (1998).
Crystallization and preliminary X-ray crystallographic studies on apolipoprotein H (beta2-glycoprotein-I) from human plasma.
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9914209 C.H.Cheng (1998).
Evolution of the diverse antifreeze proteins.
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Binding steps of apolipoprotein A-I with phospholipid monolayers: adsorption and penetration.
  Biochemistry, 37, 16165-16171.  
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Importance of central alpha-helices of human apolipoprotein A-I in the maturation of high-density lipoproteins.
  Biochemistry, 37, 13902-13909.  
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Studies of synthetic peptides of human apolipoprotein A-I containing tandem amphipathic alpha-helixes.
  Biochemistry, 37, 10313-10324.  
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