Pure and Applied Chemistry

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• Hong Zhenmin, Ahmed Zeeshan, Asher Sanford A.: Circular Dichroism and Ultraviolet Resonance Raman Indicate Little Arg-Glu Side Chain α-Helix Peptide Stabilization. J Phys Chem B 2011, 115, 4234. <http://dx.doi.org/10.1021/jp112238q>
• DE LAURETO PATRIZIA POLVERINO, TOMA SALVATORE, TONON GIANCARLO, FONTANA ANGELO: Probing the structure of human growth hormone by limited proteolysis. International journal of peptide & protein research 2009, 45, 200. <http://dx.doi.org/10.1111/j.1399-3011.1995.tb01041.x>
• Chakrabartty Avijit, Kortemme Tanja, Baldwin Robert L.: Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Sci 2008, 3, 843. <http://dx.doi.org/10.1002/pro.5560030514>
• Finkelstein A.V., Galzitskaya O.V.: Physics of protein folding. Phys Life Rev 2004, 1, 23. <http://dx.doi.org/10.1016/j.plrev.2004.03.001>
• Ptitsyn Oleg B, Ting Kai-Li H: Non-functional conserved residues in globins and their possible role as a folding nucleus. Journal of Molecular Biology 1999, 291, 671. <http://dx.doi.org/10.1006/jmbi.1999.2920>
• Ptitsyn Oleg B.: Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes?. Journal of Molecular Biology 1998, 278, 655. <http://dx.doi.org/10.1006/jmbi.1997.1620>
• Yang Jianxin, Spek Erik J., Gong Youxiang, Zhou Hongxing, Kallenbach Neville R.: The role of context on α-helix stabilization: Host-guest analysis in a mixed background peptide model. Protein Sci 1997, 6, 1264. <http://dx.doi.org/10.1002/pro.5560060614>
• Doig Andrew J., Baldwin Robert L.: N- and C-capping preferences for all 20 amino acids in α-helical peptides. Protein Sci 1995, 4, 1325. <http://dx.doi.org/10.1002/pro.5560040708>
• Monera Oscar D., Sereda Terrance J., Zhou Nian E., Kay Cyril M., Hodges Robert S.: Relationship of sidechain hydrophobicity and α-helical propensity on the stability of the single-stranded amphipathic α-helix. J Peptide Sci 1995, 1, 319. <http://dx.doi.org/10.1002/psc.310010507>
• Ptitsyn O.B, Uversky V.N: The molten globule is a third thermodynamical state of protein molecules. FEBS Letters 1994, 341, 15. <http://dx.doi.org/10.1016/0014-5793(94)80231-9>
• Oobatake Motohisa, Ooi Tatsuo: Hydration and heat stability effects on protein unfolding. Prog Biophys Molec Biol 1993, 59, 237. <http://dx.doi.org/10.1016/0079-6107(93)90002-2>
• Finkelstein A. V., Badretdinov A. Y., Ptitsyn O. B.: Physical reasons for secondary structure stability: α-Helices in short peptides. Proteins 1991, 10, 287. <http://dx.doi.org/10.1002/prot.340100403>
• Ptitsyn Oleg B., Finkelstein Alexey V.: Why do globular proteins fit the limited set of foldin patterns?. Prog Biophys Molec Biol 1987, 50, 171. <http://dx.doi.org/10.1016/0079-6107(87)90013-7>
• Ptitsyn O.B.: Random sequences and protein folding. Journal of Molecular Structure: THEOCHEM 1985, 123, 45. <http://dx.doi.org/10.1016/0166-1280(85)80191-3>
• Hol Wim G.J., Sansom M.S.P., Stuart D.I., Acharya K.R., Hajdu J., McLaughlin P.J., Johnson L.N., Ptitsyn O.B.: The variable effective dielectric constant and the importance of the direction of the peptide dipole moment: an investigation of dipole���dipole interactions in ����- and ������-units of proteins. Journal of Molecular Structure: THEOCHEM 1985, 24, 27. <http://dx.doi.org/10.1016/0166-1280(85)85183-6>
• Ptitsyn O. B., Finkelstein A. V.: Theory of protein secondary structure and algorithm of its prediction. Biopolymers (Biospectroscopy) 1983, 22, 15. <http://dx.doi.org/10.1002/bip.360220105>
• Finkelstein Alexei V., Bendzko Peter, Rapoport Tom A.: Recognition of signal sequences. FEBS Letters 1983, 161, 176. <http://dx.doi.org/10.1016/0014-5793(83)81002-3>
• Ptitsyn O. B., Finkelstein A. V.: Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding?. Quart Rev Biophys 1980, 13, 339. <http://dx.doi.org/10.1017/S0033583500001724>
• Ptitsyn O. B., Finkelstein A. V.: Mechanism of protein folding. Int J Quantum Chem 1979, 16, 407. <http://dx.doi.org/10.1002/qua.560160302>
• Finkelstein A. V., Ptitsyn O. B.: Theory of protein molecule self-organization. I. Thermodynamic parameters of local secondary structures in the unfolded protein chain. Biopolymers (Biospectroscopy) 1977, 16, 469. <http://dx.doi.org/10.1002/bip.1977.360160302>
• Finkelstein A. V., Ptitsyn O. B., Kozitsyn S. A.: Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments. Biopolymers (Biospectroscopy) 1977, 16, 497. <http://dx.doi.org/10.1002/bip.1977.360160303>
• Pfeil W., Privalov P.L.: Thermodynamic investigations of proteins. biophys chem 1976, 4, 23. <http://dx.doi.org/10.1016/0301-4622(76)80003-8>
• Ptitsyn O.B.: Invariant features of globin primary structure and coding of their secondary structure. Journal of Molecular Biology 1974, 88, 287. <http://dx.doi.org/10.1016/0022-2836(74)90482-3>