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Pure Appl. Chem., 1992, Vol. 64, No. 8, pp. 1061-1066

http://dx.doi.org/10.1351/pac199264081061

The design and construction of synthetic protein mimics

P. Balaram

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  • Ramesh Veera V.E., Priya Gowri, Rajamohanan P.R., Hofmann Hans-Jörg, Sanjayan Gangadhar J.: Expanding the structural repertoire of β/α Ant-Pro (anthranilic acid-proline) oligomers into γ/α 2-Amb-Pro (2-aminomethyl benzoic acid-proline) oligomers. Tetrahedron 2012, 68, 4399. <http://dx.doi.org/10.1016/j.tet.2012.02.006>
  • Lansac Yves, Glaser Matthew A., Maiti Prabal K., Kumar Hemant: Biopolymers in nanopores: challenges and opportunities. Soft Matt 2011, 7, 5898. <http://dx.doi.org/10.1039/c0sm01517b>
  • Roy Arup, Prabhakaran Panchami, Baruah Pranjal Kumar, Sanjayan Gangadhar J.: Diversifying the structural architecture of synthetic oligomers: the hetero foldamer approach. Chem Commn 2011, 47, 11593. <http://dx.doi.org/10.1039/c1cc13313f>
  • Sarojini Vijayalekshmi, Balaji Rao R., Ragothama S., Balaram Padmanabhan: Solution conformation of a tetradecapeptide stabilized by two di-n-propyl glycine residues. J Peptide Sci 2010, n/a. <http://dx.doi.org/10.1002/psc.1259>
  • DATTA S., SHAMALA N., GURUNATH R., BALARAM P.: Observation of a mixed antiparallel and parallel β-sheet motif in the crystal structure of Boc-Ala-Ile-Aib-OMe. Int J Peptide Protein Res 2009, 48, 209. <http://dx.doi.org/10.1111/j.1399-3011.1996.tb00833.x>
  • DATTA SAUMEN, SHAMALA N., BANERJEE ARINDAM, BALARAM P.: Hydrogen bonding in peptide helices Analysis of two independent helices in the crystal structure of a peptide Boc-Val-Ala-Leu-Aib-Val-Ala-Phe-OMe. J Pept Res 2009, 49, 604. <http://dx.doi.org/10.1111/j.1399-3011.1997.tb01169.x>
  • Balaram P.: De novo design: backbone conformational constraints in nucleating helices andβ-hairpins : Conformational constraints in nucleating helices and β-hairpins. J Pept Res 2008, 54, 195. <http://dx.doi.org/10.1034/j.1399-3011.1999.00119.x>
  • Honda Takeshi, Miyazaki Masaya, Yamaguchi Yoshiko, Nakamura Hiroyuki, Maeda Hideaki: Integrated microreaction system for optical resolution of racemic amino acids. Lab Chip 2007, 7, 366. <http://dx.doi.org/10.1039/b614500k>
  • Karle Isabella L., Das Chittaranjan, Balaram P.: Effects of hydrogen-bond deletion on peptide helices: Structural characterization of depsipeptides containing lactic acid. Biopolymers (Biospectroscopy) 2001, 59, 276. <http://dx.doi.org/10.1002/1097-0282(20011005)59:4<276::AID-BIP1024>3.0.CO;2-X>
  • Das Chittaranjan, Shankaramma S. Channaveerappa, Balaram Padmanabhan: Molecular Carpentry: Piecing Together Helices and Hairpins in Designed Peptides. Chem Eur J 2001, 7, 840. <http://dx.doi.org/10.1002/1521-3765(20010216)7:4<840::AID-CHEM840>3.0.CO;2-M>
  • Ramagopal U. A., Ramakumar S., Sahal D., Chauhan V. S.: De novo design and characterization of an apolar helical hairpin peptide at atomic resolution: Compaction mediated by weak interactions. Proceedings of the National Academy of Sciences 2001, 98, 870. <http://dx.doi.org/10.1073/pnas.98.3.870>
  • Karle I. L., Das C., Balaram P.: De novo protein design: Crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains. Proceedings of the National Academy of Sciences 2000, 97, 3034. <http://dx.doi.org/10.1073/pnas.97.7.3034>
  • Karle Isabella L., Rao R. Balaji, Kaul Ramesh, Prasad Sudhanand, Balaram P.: Peptide design: Crystal structure of a helical peptide module attached to a potentially nonhelical amino terminal segment. Biopolymers (Biospectroscopy) 1998, 39, 75. <http://dx.doi.org/10.1002/(SICI)1097-0282(199607)39:1<75::AID-BIP8>3.0.CO;2-S>
  • Ananda Kuppanna, Gopi Hosahudya N., Suresh Babu Vommina V.: Rapid and efficient synthesis of peptides containing α,α-dialkylamino acids employing KOBt. Lett Peptide Sci 1998, 5, 277. <http://dx.doi.org/10.1007/BF02443545>
  • Karle Isabella L, Banerjee Arindam, Balaram Padmanabhan: Design of two-helix motifs in peptides: crystal structure of a system of linked helices of opposite chirality and a model helix���linker peptide. Folding and Design 1997, 2, 203. <http://dx.doi.org/10.1016/S1359-0278(97)00029-1>
  • Toniolo Claudio, Bianco Alberto, Formaggio Fernando, Crisma Marco, Bonora Gian Maria, Benedetti Ettore, Del Duca Valerio, Saviano Michele, Di Blasio Benedetto, Pedone Carlo: The polypeptide 310-helix as a template for molecular recognition studies. Structural characterization of a sidechain functionalized octapeptide. biorg med chem 1995, 3, 1211. <http://dx.doi.org/10.1016/0968-0896(95)00109-T>
  • Betz Stephen F., Raleigh Daniel P., DeGrado William F.: De novo protein design: from molten globules to native-like states. curr opin struct biol 1993, 3, 601. <http://dx.doi.org/10.1016/0959-440X(93)90090-8>
  • Toniolo Claudio, Formaggio Fernando, Crisma Marco, Valle Giovanni, Boesten Wilhelmus H.J., Schoemaker Hans E., Kamphuis Johan, Temussi Piero A., Becker Elmer L., Précigoux Gilles: Bioactive and model peptides characterized by the helicogenic (αMe)Phe residue. Tetrahedron 1993, 49, 3641. <http://dx.doi.org/10.1016/S0040-4020(01)90220-0>
  • Balaram Padmanabhan: Non-standard amino acids in peptide design and protein engineering. curr opin struct biol 1992, 2, 845. <http://dx.doi.org/10.1016/0959-440X(92)90110-S>