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1
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0000478078
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Templates that induce α-helical, β-sheet, and loop conformations
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Schneider J.P., Kelly J.W. Templates that induce α-helical, β-sheet, and loop conformations. Chem Rev. 95:1995;2169-2187.
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Schneider, J.P.1
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0031152163
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Soth M.J., Nowick J.S. Unnatural oligomers and unnatural oligomer libraries. Curr Opin Chem Biol. 1:1997;120-129.
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0542421525
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Foldamers: A manifesto
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An excellent review of oligomers that fold into defined structures. Gellman not only discusses the folding oligomers reported before 1998, but also describes much of the intellectual framework behind this area of research and potential applications of these molecules
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Gellman S.H. Foldamers: a manifesto. Acc Chem Res. 31:1998;173-180. An excellent review of oligomers that fold into defined structures. Gellman not only discusses the folding oligomers reported before 1998, but also describes much of the intellectual framework behind this area of research and potential applications of these molecules.
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Acc Chem Res
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Gellman, S.H.1
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4
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0029856721
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Probing the helical secondary structure of short-chain β-peptides
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Seebach D., Ciceri P.E., Overhand M., Jaun B., Rigo D., Oberer L., Hommel U., Amstutz R., Widmer H. Probing the helical secondary structure of short-chain β-peptides. Helv Chim Acta. 79:1996;2043-2066.
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Helv Chim Acta
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Seebach, D.1
Ciceri, P.E.2
Overhand, M.3
Jaun, B.4
Rigo, D.5
Oberer, L.6
Hommel, U.7
Amstutz, R.8
Widmer, H.9
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5
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0029953285
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β-Peptides: Synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a β-hexapeptide in solution and its stability towards pepsin
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Seebach D., Overhand M., Kühnle F.N.M., Martinoni B., Oberer L., Hommel U., Widmer H. β-Peptides: synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a β-hexapeptide in solution and its stability towards pepsin. Helv Chim Acta. 79:1996;913-941.
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Helv Chim Acta
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Seebach, D.1
Overhand, M.2
Kühnle, F.N.M.3
Martinoni, B.4
Oberer, L.5
Hommel, U.6
Widmer, H.7
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6
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0030461803
-
β-Peptide foldamers: Robust helix formation in a new family of β-amino acid oligomers
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Appella D.H., Christianson L.A., Karle I.L., Powell D.R., Gellman S.H. β-Peptide foldamers: robust helix formation in a new family of β-amino acid oligomers. J Am Chem Soc. 118:1996;13071-13072.
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Appella, D.H.1
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Karle, I.L.3
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Gellman, S.H.5
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7
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0033532930
-
Synthesis and characterization of trans-2-aminocyclo-hexanecarboxylic acid oligomers: An unnatural helical secondary structure and implications for β-peptide tertiary structure
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14 helix with side-to-side packing interactions reminiscent of a three-helix bundle, and suggest that amphiphilic helices could form tertiary structure
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14 helix with side-to-side packing interactions reminiscent of a three-helix bundle, and suggest that amphiphilic helices could form tertiary structure.
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J Am Chem Soc
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Appella, D.H.1
Christianson, L.A.2
Karle, I.L.3
Powell, D.R.4
Gellman, S.H.5
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8
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-
0033577324
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Formation of short, stable, helices in aqueous solution by β-amino acid hexamers
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A water soluble β-hexamer containing functionality found in natural peptides is described. The hexamer is predominantly helical (90%) in aqueous solution. A series of β-hexamers with an increasing number of acyclic side chains was compared by circular dichroism spectroscopy. Cyclic side chains were thus shown to be essential for a stable helical structure in water
-
Appella D.H., Barchi J.J., Durell S.R., Gellman S.H. Formation of short, stable, helices in aqueous solution by β-amino acid hexamers. J Am Chem Soc. 121:1999;2309-2310. A water soluble β-hexamer containing functionality found in natural peptides is described. The hexamer is predominantly helical (90%) in aqueous solution. A series of β-hexamers with an increasing number of acyclic side chains was compared by circular dichroism spectroscopy. Cyclic side chains were thus shown to be essential for a stable helical structure in water.
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J Am Chem Soc
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Appella, D.H.1
Barchi, J.J.2
Durell, S.R.3
Gellman, S.H.4
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10
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0001452530
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3-peptides with proteinaceous side chains: Synthesis and solution structures of constitutional isomers, a novel helical secondary structure and the influence of solvation and hydrophobic interactions on folding
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•].
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•].
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(1998)
Helv Chim Acta
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Seebach, D.1
Abele, S.2
Gademann, K.3
Guichard, G.4
Hintermann, T.5
Jaun, B.6
Matthews, J.L.7
Schreiber, J.V.8
Oberer, L.9
Hommel, U.10
Widmer, H.11
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11
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0033168016
-
Nonapeptide analogues containing (R)-3-hydroxybutanoate and β-homoalanine oligomers: Synthesis and binding affinity to a class I major histocompatability complex protein
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Poenaru S., Lamas J.R., Folkers G., Lóez de Castro J.A., Seebach D., Rognan D. Nonapeptide analogues containing (R)-3-hydroxybutanoate and β-homoalanine oligomers: synthesis and binding affinity to a class I major histocompatability complex protein. J Med Chem. 42:1999;2318-2331.
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Poenaru, S.1
Lamas, J.R.2
Folkers, G.3
Lóez De Castro, J.A.4
Seebach, D.5
Rognan, D.6
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12
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0032569174
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Design of secondary structures in unnatural peptides: Stable helical γ-tetra, hexa-, and octapeptides and consequences of α-substitution
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Hanessian S., Luo X., Schaum R., Michnick S. Design of secondary structures in unnatural peptides: stable helical γ-tetra, hexa-, and octapeptides and consequences of α-substitution. J Am Chem Soc. 120:1998;8569-8570.
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Hanessian, S.1
Luo, X.2
Schaum, R.3
Michnick, S.4
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13
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0033516710
-
Synthesis and folding preferences of γ-amino acid oligopeptides: Stereochemical control in the formation of a reverse turn and a helix
-
The authors describe a γ-peptide turn structure. The substitution pattern originally reported in [12] as 'non-helical' appears to adopt a turn structure instead
-
Hanessian S., Luo X., Schaum R. Synthesis and folding preferences of γ-amino acid oligopeptides: stereochemical control in the formation of a reverse turn and a helix. Tetrahedron Lett. 40:1999;4925-4929. The authors describe a γ-peptide turn structure. The substitution pattern originally reported in [12] as 'non-helical' appears to adopt a turn structure instead.
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Tetrahedron Lett
, vol.40
, pp. 4925-4929
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Hanessian, S.1
Luo, X.2
Schaum, R.3
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15
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-
0032911804
-
Chemical models of protein β-sheets
-
This review paper is an excellent overview of Nowick's work on the synthesis and study of artificial β-sheet structures
-
Nowick J.S. Chemical models of protein β-sheets. Acc Chem Res. 32:1999;287-296. This review paper is an excellent overview of Nowick's work on the synthesis and study of artificial β-sheet structures.
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Acc Chem Res
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, pp. 287-296
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Nowick, J.S.1
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16
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0032505197
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An efficient synthesis of N,N′-linked oligoureas
-
An efficient sub-monomer approach to the synthesis of N,N′-linked oligoureas is described
-
Wilson M.E., Nowick J.S. An efficient synthesis of N,N′-linked oligoureas. Tetrahedron Lett. 39:1998;6613-6616. An efficient sub-monomer approach to the synthesis of N,N′-linked oligoureas is described.
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Tetrahedron Lett
, vol.39
, pp. 6613-6616
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-
Wilson, M.E.1
Nowick, J.S.2
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17
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0033608075
-
Novel turns and helices in peptides of chiral α-aminoxy acids
-
The authors describe the synthesis and structural studies of α-aminoxy acids. α-Aminoxy acids access a conformation that is unavailable to their β-amino acid isosteres, a very tight helix that appears to be preferred even by short oligomers and is independent of sidechain identity.
-
Yang D., Qu J., Li B., Ng F.-F., Wang X.-C., Cheung K.-K., Wang D.-P., Wu Y.-D. Novel turns and helices in peptides of chiral α-aminoxy acids. J Am Chem Soc. 121:1999;589-590. The authors describe the synthesis and structural studies of α-aminoxy acids. α-Aminoxy acids access a conformation that is unavailable to their β-amino acid isosteres, a very tight helix that appears to be preferred even by short oligomers and is independent of sidechain identity.
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(1999)
J Am Chem Soc
, vol.121
, pp. 589-590
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Yang, D.1
Qu, J.2
Li, B.3
Ng, F.-F.4
Wang, X.-C.5
Cheung, K.-K.6
Wang, D.-P.7
Wu, Y.-D.8
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18
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0033553120
-
Flat peptides
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Crisma M., Formaggio F., Toniolo C., Yoshikawa T., Wakamiya T. Flat peptides. J Am Chem Soc. 121:1999;3272-3278.
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J Am Chem Soc
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Crisma, M.1
Formaggio, F.2
Toniolo, C.3
Yoshikawa, T.4
Wakamiya, T.5
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19
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0344515255
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Secondary structure in oligomers of carbohydrate amino acids
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•]. The 1,4-cis-furanosides form a repeated 'β-turn' helix with some fraying at the carboxyl terminus as the ester group cannot participate in the hydrogen-bonding structure
-
•]. The 1,4-cis-furanosides form a repeated 'β-turn' helix with some fraying at the carboxyl terminus as the ester group cannot participate in the hydrogen-bonding structure.
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Chem Commun
, pp. 2041-2042
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Smith, M.D.1
Claridge, T.D.W.2
Tranter, G.E.3
Sansom, M.S.P.4
Fleet, G.W.J.5
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20
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0032506688
-
A solid phase approach to oligomers of carbohydrate amino-acids: Secondary structure in a trimeric furanose carbopeptoid
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•] was stabilized by replacing the carboxy-terminal ester with an amide to allow the end to participate in hydrogen-bonded turn formation
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•] was stabilized by replacing the carboxy-terminal ester with an amide to allow the end to participate in hydrogen-bonded turn formation.
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(1998)
Tetrahedron Lett
, vol.39
, pp. 9293-9296
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Long, D.D.1
Smith, M.D.2
Marquess, D.G.3
Claridge, T.D.W.4
Fleet, G.W.J.5
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21
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-
0033548539
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An octameric carbopeptoid; Secondary structure in octameric and tetrameric 5-aminomethyl-tetrahydrofuran-2-carboxylates
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•], the octamer prefers a different folded conformation. This is a common theme in the amino acid homologues: differing substitution patterns result in different structures
-
•], the octamer prefers a different folded conformation. This is a common theme in the amino acid homologues: differing substitution patterns result in different structures.
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(1999)
Tetrahedron Lett
, vol.40
, pp. 2199-2202
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-
Claridge, T.D.W.1
Long, D.D.2
Hungerford, N.L.3
Aplin, R.T.4
Smith, M.D.5
Marquess, D.G.6
Fleet, G.W.J.7
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22
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0000496054
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Solid phase synthesis and secondary structural studies of (1-5) amide-linked sialooligomers
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Szabo L., Smith B.L., McReynolds K.D., Parill A.L., Morris E.R., Gervay J. Solid phase synthesis and secondary structural studies of (1-5) amide-linked sialooligomers. J Org Chem. 63:1998;1074-1078.
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Szabo, L.1
Smith, B.L.2
McReynolds, K.D.3
Parill, A.L.4
Morris, E.R.5
Gervay, J.6
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23
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0029759396
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Oligoanthranilamides. Non-peptide subunits that show formation of specific secondary structure
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Hamuro Y., Geib S.J., Hamilton A.D. Oligoanthranilamides. Non-peptide subunits that show formation of specific secondary structure. J Am Chem Soc. 118:1996;7529-7541.
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J Am Chem Soc
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Hamuro, Y.1
Geib, S.J.2
Hamilton, A.D.3
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24
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0030838308
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Novel folding patterns in a family of oligoanthranilamides: Non-peptide oligomers that form extended helical secondary structures
-
Describes structures composed of three separate subunits: anthranilamide, pyridine-2,6-dicarboxylic acid, and 1,5-diamino-2,4-dimethoxybenzene. These subunits are combined in carefully chosen sequences, and the resultant hybrids can form extended strands, turns, or helices
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Hamuro Y., Geib S.J., Hamilton A.D. Novel folding patterns in a family of oligoanthranilamides: non-peptide oligomers that form extended helical secondary structures. J Am Chem Soc. 119:1997;10587-10593. Describes structures composed of three separate subunits: anthranilamide, pyridine-2,6-dicarboxylic acid, and 1,5-diamino-2,4-dimethoxybenzene. These subunits are combined in carefully chosen sequences, and the resultant hybrids can form extended strands, turns, or helices.
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J Am Chem Soc
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Hamuro, Y.1
Geib, S.J.2
Hamilton, A.D.3
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25
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0032515982
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Sequence-specific polypeptoids: A diverse family of heteropolymers with stable secondary structure
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The authors describe the structure of oligomeric N-alkylglycines (peptoids). Peptoids have a well-defined helical structure, even in water, because the structure is independent of hydrogen bonding. The helicity depends on the chirality of the side chains, and on the length of the oligomer
-
Kirshenbaum K., Barron A.E., Goldsmith R.A., Armand P., Bradley E.K., Truong K.T.V., Dill K.A., Cohen F.E., Zuckermann R.N. Sequence-specific polypeptoids: a diverse family of heteropolymers with stable secondary structure. Proc Natl Acad Sci USA. 95:1998;4303-4308. The authors describe the structure of oligomeric N-alkylglycines (peptoids). Peptoids have a well-defined helical structure, even in water, because the structure is independent of hydrogen bonding. The helicity depends on the chirality of the side chains, and on the length of the oligomer.
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(1998)
Proc Natl Acad Sci USA
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Kirshenbaum, K.1
Barron, A.E.2
Goldsmith, R.A.3
Armand, P.4
Bradley, E.K.5
Truong, K.T.V.6
Dill, K.A.7
Cohen, F.E.8
Zuckermann, R.N.9
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26
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13144306061
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NMR determination of the major solution conformation of a peptoid pentamer with chiral side chains
-
Armand P., Kirshenbaum K., Goldsmith R.A., Farr-Jones S., Barron A.E., Truong K.T.V., Dill K.A., Mierke D.F., Cohen F.E., Zuckermann R.N., Bradley E.K. NMR determination of the major solution conformation of a peptoid pentamer with chiral side chains. Proc Natl Acad Sci USA. 95:1998;4309-4314.
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Proc Natl Acad Sci USA
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Armand, P.1
Kirshenbaum, K.2
Goldsmith, R.A.3
Farr-Jones, S.4
Barron, A.E.5
Truong, K.T.V.6
Dill, K.A.7
Mierke, D.F.8
Cohen, F.E.9
Zuckermann, R.N.10
Bradley, E.K.11
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27
-
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0032509175
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Exploiting the basis of proline recognition by SH3 and WW domains: Design of N-substituted inhibitors
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Nguyen J.T., Turck C.W., Cohen R.E., Zuckermann R.N., Lim W.A. Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors. Science. 282:1998;2088-2092.
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Science
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Nguyen, J.T.1
Turck, C.W.2
Cohen, R.E.3
Zuckermann, R.N.4
Lim, W.A.5
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28
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0030823475
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Solvophobically driven folding of nonbiological oligomers
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Nelson J.C., Saven J.G., Moore J.S., Wolynes P.G. Solvophobically driven folding of nonbiological oligomers. Science. 277:1997;1793-1796.
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Nelson, J.C.1
Saven, J.G.2
Moore, J.S.3
Wolynes, P.G.4
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29
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0033531714
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Cooperative conformational transitions in phenylene ethynylene oligomers: Chain length dependence
-
This paper describes spectroscopic studies of phenylene ethynylene oligomers that demonstrate that the folding of these oligomers depends on solvent effects and chain length. The oligomers fold in polar solvents, and ten or more monomer units are required for folding
-
Prince R.B., Saven J.G., Wolynes P.G., Moore J.S. Cooperative conformational transitions in phenylene ethynylene oligomers: chain length dependence. J Am Chem Soc. 121:1999;3114-3121. This paper describes spectroscopic studies of phenylene ethynylene oligomers that demonstrate that the folding of these oligomers depends on solvent effects and chain length. The oligomers fold in polar solvents, and ten or more monomer units are required for folding.
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J Am Chem Soc
, vol.121
, pp. 3114-3121
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Prince, R.B.1
Saven, J.G.2
Wolynes, P.G.3
Moore, J.S.4
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30
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0033555217
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Controlling the secondary structure of nonbiological oligomers with solvophobic and coordination interactions
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Prince R.B., Okada T., Moore J.S. Controlling the secondary structure of nonbiological oligomers with solvophobic and coordination interactions. Angew Chem Int Ed Engl. 38:1999;233-236.
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Angew Chem Int Ed Engl
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Prince, R.B.1
Okada, T.2
Moore, J.S.3
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31
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0033599526
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Helical bias in solvophobically folded oligo(phenylene ethynylene)s
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Gin M.S., Yokozawa T., Prince R.B., Moore J.S. Helical bias in solvophobically folded oligo(phenylene ethynylene)s. J Am Chem Soc. 121:1999;2643-2644.
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J Am Chem Soc
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Gin, M.S.1
Yokozawa, T.2
Prince, R.B.3
Moore, J.S.4
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32
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0032820462
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Conformational preferences of peptides containing reverse-turn mimetic bicyclic lactams: Inverse γ-turns versus type-II′ β-turns - insights into β-hairpin stability
-
This paper contains an excellent discussion of solution structure determination, with an outstanding discussion of hydrogen bonding studies using various NMR techniques (chemical shift, temperature dependence, solvent dependence)
-
Belvisi L., Gennari C., Mielgo A., Potenza D., Scolastico C. Conformational preferences of peptides containing reverse-turn mimetic bicyclic lactams: inverse γ-turns versus type-II′ β-turns - insights into β-hairpin stability. Eur J Org Chem. 1999;389-400. This paper contains an excellent discussion of solution structure determination, with an outstanding discussion of hydrogen bonding studies using various NMR techniques (chemical shift, temperature dependence, solvent dependence).
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(1999)
Eur J Org Chem
, pp. 389-400
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Belvisi, L.1
Gennari, C.2
Mielgo, A.3
Potenza, D.4
Scolastico, C.5
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33
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0011034289
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Hydrophobic cluster formation is necessary for dibenzofuran-based amino acids to function as β-sheet nucleators
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Tsang K.Y., Diaz H., Graciani N., Kelly J.W. Hydrophobic cluster formation is necessary for dibenzofuran-based amino acids to function as β-sheet nucleators. J Am Chem Soc. 116:1994;3988-4005.
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Tsang, K.Y.1
Diaz, H.2
Graciani, N.3
Kelly, J.W.4
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34
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0032978519
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The nucleation of monomeric parallel β-sheet-like structures and their self-assembly in aqueous solution
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Chitnumsub P., Fiori W.R., Lashuel H.A., Diaz H., Kelly J.W. The nucleation of monomeric parallel β-sheet-like structures and their self-assembly in aqueous solution. Bioorg Med Chem. 7:1999;39-59.
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Bioorg Med Chem
, vol.7
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Chitnumsub, P.1
Fiori, W.R.2
Lashuel, H.A.3
Diaz, H.4
Kelly, J.W.5
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35
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0033534574
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A peptide/oligourea/azapeptide hybrid that adopts a hairpin turn
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Soth M.J., Nowick J.S. A peptide/oligourea/azapeptide hybrid that adopts a hairpin turn. J Org Chem. 64:1999;276-281.
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J Org Chem
, vol.64
, pp. 276-281
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Soth, M.J.1
Nowick, J.S.2
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36
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0032569180
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Demonstration of endo-cis-(2S,3R)-bicyclo[2.2.1]hept-5-en-2,3-dicarbonyl unit as a reverse-turn scaffold and nucleator of two-stranded parallel β-sheets: Design, synthesis, crystal structure, and self-assembling properties of norborneno peptide analogues
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Ranganathan D., Haridas V., Kurur S., Thomas A., Madhusudanan K.P., Nagaraj R., Kunwar A.C., Sarma A.V.S., Karle I.L. Demonstration of endo-cis-(2S,3R)-bicyclo[2.2.1]hept-5-en-2,3-dicarbonyl unit as a reverse-turn scaffold and nucleator of two-stranded parallel β-sheets: design, synthesis, crystal structure, and self-assembling properties of norborneno peptide analogues. J Am Chem Soc. 120:1998;8448-8460.
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(1998)
J Am Chem Soc
, vol.120
, pp. 8448-8460
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-
Ranganathan, D.1
Haridas, V.2
Kurur, S.3
Thomas, A.4
Madhusudanan, K.P.5
Nagaraj, R.6
Kunwar, A.C.7
Sarma, A.V.S.8
Karle, I.L.9
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37
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0001099564
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Conformational analysis of peptides and pseudopeptides incorporating an endo-(2S,3R)-norborn-5-ene residue as a turn inducer
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Jones I.G., Jones W., North M. Conformational analysis of peptides and pseudopeptides incorporating an endo-(2S,3R)-norborn-5-ene residue as a turn inducer. J Org Chem. 63:1998;1505-1513.
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J Org Chem
, vol.63
, pp. 1505-1513
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Jones, I.G.1
Jones, W.2
North, M.3
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38
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0033011780
-
Molecular modeling, synthesis, and structures of N-methylated 3,5-linked pyrrolin-4-ones toward the creation of a privileged nonpeptide scaffold
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Smith A.B. III, Favor D.A., Sprengeler P.A., Guzman M.C., Carroll P.J., Furst G.T., Hirschmann R. Molecular modeling, synthesis, and structures of N-methylated 3,5-linked pyrrolin-4-ones toward the creation of a privileged nonpeptide scaffold. Bioorg Med Chem. 7:1999;9-22.
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Bioorg Med Chem
, vol.7
, pp. 9-22
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-
Smith A.B. III1
Favor, D.A.2
Sprengeler, P.A.3
Guzman, M.C.4
Carroll, P.J.5
Furst, G.T.6
Hirschmann, R.7
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39
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0029139422
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An achiral dipeptide mimetic that promotes β-hairpin formation
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Gardner R.R., Liang G.-B., Gellman S.H. An achiral dipeptide mimetic that promotes β-hairpin formation. J Am Chem Soc. 117:1995;3280-3281.
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(1995)
J Am Chem Soc
, vol.117
, pp. 3280-3281
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Gardner, R.R.1
Liang, G.-B.2
Gellman, S.H.3
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41
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0033541110
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β-Turn and β-hairpin mimicry with tetrasubstituted alkenes
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This paper contains a full study of the Gellman group's acyclic β-turn mimic reported in [39] and investigates the alternative conformations accessed by peptide strands containing this turn unit
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Gardner R.R., Liang G.-B., Gellman S.H. β-Turn and β-hairpin mimicry with tetrasubstituted alkenes. J Am Chem Soc. 121:1999;1806-1816. This paper contains a full study of the Gellman group's acyclic β-turn mimic reported in [39] and investigates the alternative conformations accessed by peptide strands containing this turn unit.
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(1999)
J Am Chem Soc
, vol.121
, pp. 1806-1816
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Gardner, R.R.1
Liang, G.-B.2
Gellman, S.H.3
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42
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0000428997
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Methyl- And (trifuoromethyl)alkene peptide isosteres: Synthesis and evaluation of their potential as β-turn promoters and peptide mimetics
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Wipf P., Henninger T.C., Geib S.J. Methyl- and (trifuoromethyl)alkene peptide isosteres: synthesis and evaluation of their potential as β-turn promoters and peptide mimetics. J Org Chem. 63:1998;6088-6089.
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(1998)
J Org Chem
, vol.63
, pp. 6088-6089
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Wipf, P.1
Henninger, T.C.2
Geib, S.J.3
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43
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0032517330
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A β-peptide reverse turn that promotes hairpin formation
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The authors describe a heterochiral nipecotic acid dimer that nucleates β-hairpin turns. Interestingly, the homochiral nipecotic dimer does not exhibit the internal hydrogen bonding required for a turn. In conjunction with previous studies, this study confirms that β-peptides can access all three protein secondary structures
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Chung Y.J., Christianson L.A., Stanger H.E., Powell D.R., Gellman S.H. A β-peptide reverse turn that promotes hairpin formation. J Am Chem Soc. 120:1998;10555-10556. The authors describe a heterochiral nipecotic acid dimer that nucleates β-hairpin turns. Interestingly, the homochiral nipecotic dimer does not exhibit the internal hydrogen bonding required for a turn. In conjunction with previous studies, this study confirms that β-peptides can access all three protein secondary structures.
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(1998)
J Am Chem Soc
, vol.120
, pp. 10555-10556
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Chung, Y.J.1
Christianson, L.A.2
Stanger, H.E.3
Powell, D.R.4
Gellman, S.H.5
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45
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0032431413
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3,3-amino acids: A turn motif for β-peptides
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3,3-amino acids: a turn motif for β-peptides. Helv Chim Acta. 81:1998;2218-2243.
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(1998)
Helv Chim Acta
, vol.81
, pp. 2218-2243
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Seebach, D.1
Abele, S.2
Sifferlen, T.3
Hänggi, M.4
Gruner, S.5
Seiler, P.6
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47
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0033515624
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Folding of an artificial β-sheet in competitive solvents
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Junquera E., Nowick J.S. Folding of an artificial β-sheet in competitive solvents. J Org Chem. 64:1999;2527-2531.
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(1999)
J Org Chem
, vol.64
, pp. 2527-2531
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Junquera, E.1
Nowick, J.S.2
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49
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0033568016
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A chemical model of a protein β-sheet dimer
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The authors describe the synthesis of a β-sheet mimic that dimerizes. This result suggests that similar compounds can be designed to interfere with the β-sheets formed at protein-protein interfaces
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Nowick J.S., Tsai J.H., Bui Q.-C.D., Maitra S. A chemical model of a protein β-sheet dimer. J Am Chem Soc. 121:1999;8409-8410. The authors describe the synthesis of a β-sheet mimic that dimerizes. This result suggests that similar compounds can be designed to interfere with the β-sheets formed at protein-protein interfaces.
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(1999)
J Am Chem Soc
, vol.121
, pp. 8409-8410
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Nowick, J.S.1
Tsai, J.H.2
Bui, Q.-C.D.3
Maitra, S.4
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50
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0033575070
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A new approach for the design of supramolecular recognition units: Hydrogen-bonded molecular duplexes
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Gong B., Yan Y., Zeng H., Skrzypczak-Jankunn E., Kim Y.W., Zhu J., Ickes H. A new approach for the design of supramolecular recognition units: hydrogen-bonded molecular duplexes. J Am Chem Soc. 121:1999;3007-3008.
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(1999)
J Am Chem Soc
, vol.121
, pp. 3007-3008
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Gong, B.1
Yan, Y.2
Zeng, H.3
Skrzypczak-Jankunn, E.4
Kim, Y.W.5
Zhu, J.6
Ickes, H.7
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