Pure and Applied Chemistry

CrossRef Cited-by Linking

• Jas Gouri S., Hegefeld Wendy A., Májek Peter, Kuczera Krzysztof, Elber Ron: Experiments and Comprehensive Simulations of the Formation of a Helical Turn. J. Phys. Chem. B 2012, 116, 6598. <http://dx.doi.org/10.1021/jp211645s>
• Freire Felix, Almeida Aaron M., Fisk John D., Steinkruger Jay D., Gellman Samuel H.: Impact of Strand Length on the Stability of Parallel-β-Sheet Secondary Structure. angew chemie 2011, 123, 8894. <http://dx.doi.org/10.1002/ange.201102986>
• Freire Felix, Almeida Aaron M., Fisk John D., Steinkruger Jay D., Gellman Samuel H.: Impact of Strand Length on the Stability of Parallel-β-Sheet Secondary Structure. Angew Chem Int E 2011, 50, 8735. <http://dx.doi.org/10.1002/anie.201102986>
• Mehlhorn Achim, Herzog Klaus, Noack Heike, Losse Günter: Die Natur der Protein-Protein-Wechselwirkung und ihr spektroskopischer Nachweis, dargestellt am Beispiel der Polyglycin-Insulin-Aggregate. Z Chem 2010, 30, 240. <http://dx.doi.org/10.1002/zfch.19900300703>
• Malkov Saša N., Živković Miodrag V., Beljanski Miloš V., Stojanović Srđan Đ., Zarić Snežana D.: A Reexamination of Correlations of Amino Acids with Particular Secondary Structures. Protein J 2009, 28, 74. <http://dx.doi.org/10.1007/s10930-009-9166-3>
• Lin Milo M., Shorokhov Dmitry, Zewail Ahmed H.: Helix-to-coil transitions in proteins: Helicity resonance in ultrafast electron diffraction. chem phys letts 2006, 420, 1. <http://dx.doi.org/10.1016/j.cplett.2005.11.088>
• Shi Zhengshuang, Olson C.Anders, Bell Anthony J, Kallenbach Neville R: Non-classical helix-stabilizing interactions: CH⋯O H-bonding between Phe and Glu side chains in α-helical peptides. biophys chem 2002, 101-102, 267. <http://dx.doi.org/10.1016/S0301-4622(02)00171-0>
• Scheraga Harold A., Vila Jorge A., Ripoll Daniel R.: Helix–coil transitions re-visited. biophys chem 2002, 101-102, 255. <http://dx.doi.org/10.1016/S0301-4622(02)00175-8>
• Vila Jorge A., Ripoll Daniel R., Scheraga Harold A.: Influence of lysine content and PH on the stability of alanine-based copolypeptides. Biopolymers (Biospectroscopy) 2001, 58, 235. <http://dx.doi.org/10.1002/1097-0282(200103)58:3<235::AID-BIP1001>3.0.CO;2-T>
• Merkel Jane S, Sturtevant Julian M, Regan Lynne: Sidechain interactions in parallel β sheets: the energetics of cross-strand pairings. Struct Fold Des 1999, 7, 1333. <http://dx.doi.org/10.1016/S0969-2126(00)80023-4>
• Koehl P., Levitt M.: Structure-based conformational preferences of amino acids. Proceedings of the National Academy of Sciences 1999, 96, 12524. <http://dx.doi.org/10.1073/pnas.96.22.12524>
• Gani David, Lewis Arwel, Rutherford Trevor, Wilkie John, Stirling Iain, Jenn Thierry, Ryan Martin D.: Design, synthesis, structure and properties of an α-helix cap template derived from N-[(2S)-2-chloropropionyl]-(2S)-Pro-(2R)-Ala-(2S,4S)-4-thioPro-OMe which initiates α-helical structures. Tetrahedron 1998, 54, 15793. <http://dx.doi.org/10.1016/S0040-4020(98)00991-0>
• Ptak Dave: Rigid-body oscillations of α-helices: implications for protein thermal stability. biophys chem 1998, 73, 121. <http://dx.doi.org/10.1016/S0301-4622(98)00143-4>
• Murali R., Sharkey D. J., Daiss J. L., Murthy H. M. K.: Crystal structure of Taq DNA polymerase in complex with an inhibitory Fab: The Fab is directed against an intermediate in the helix-coil dynamics of the enzyme. Proceedings of the National Academy of Sciences 1998, 95, 12562. <http://dx.doi.org/10.1073/pnas.95.21.12562>
• Lutgring R., Lipton M., Chmielewski J.: Differential self assembly of amphiphilic helical peptides. Amino Acids 1996, 10, 295. <http://dx.doi.org/10.1007/BF00805858>
• Yu Chongxi, Taylor John W.: A new strategy applied to the synthesis of an α-helical bicyclic peptide constrained by two overlapping i, i+7 side-chain bridges of novel design. Tetrahetron Lett 1996, 37, 1731. <http://dx.doi.org/10.1016/0040-4039(96)00121-9>
• Berger Jay S., Ernst James A., Nicoletta Angelo C., Hull Leslie A., Yang Jianxin, Qiu Rong, Morozov Victor N., Kallenbach Neville R.: Stabilization of Helical Peptides by Mixed Spaced Salt Bridges. Journal of Biomolecular Structure & Dynamics 1996, 14, 285. <http://dx.doi.org/10.1080/07391102.1996.10508124>
• Sturtevant Julian M.: The thermodynamic effects of protein mutations. curr opin struct biol 1994, 4, 69. <http://dx.doi.org/10.1016/S0959-440X(94)90062-0>
• Soman Kizhake V., Karimi Afshin, Case David A.: Molecular dynamics analysis of a ribonuclease C-peptide analogue. Biopolymers (Biospectroscopy) 1993, 33, 1567. <http://dx.doi.org/10.1002/bip.360331007>
• O'Shea Erin K., Lumb Kevin J., Kim Peter S.: Peptide ‘Velcro’: Design of a heterodimeric coiled coil. Current Biology 1993, 3, 658. <http://dx.doi.org/10.1016/0960-9822(93)90063-T>
• Basu Gautam, Kuki Atsuo: Conformational preferences of oligopeptides rich in α-aminoisobutyric acid. II. A model for the 310/α-helix transition with composition and sequence sensitivity. Biopolymers (Biospectroscopy) 1992, 32, 61. <http://dx.doi.org/10.1002/bip.360320109>
• Chen Chau-Chyun, Zhu Yizu, King Jonathan A., Evans Lawrence B.: A molecular thermodynamic approach to predict the secondary structure of homopolypeptides in aqueous systems. Biopolymers (Biospectroscopy) 1992, 32, 1375. <http://dx.doi.org/10.1002/bip.360321011>
• FACCHIANO Francesco, RAGONE Raffaele, PORCELLI Marina, CACCIAPUOTI Giovanna, COLONNA Giovanni: Effect of temperature on the propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium.. 1. Conformational behavior of the oligomeric enzyme in solution. Eur J Biochem 1992, 204, 473. <http://dx.doi.org/10.1111/j.1432-1033.1992.tb16657.x>
• Wójcik J., Altmann K.-H., Scheraga H. A.: Helix-coil stability constants for the naturally occurring amino acids in water. XXIV. Half-cystine parameters from random poly(hydroxybutylglutamine-CO-S-methylthio-L-cysteine). Biopolymers (Biospectroscopy) 1990, 30, 121. <http://dx.doi.org/10.1002/bip.360300113>
• Holtzer Alfred, Holtzer Marilyn Emerson: α-Helix to random-coil transitions of two-chain coiled coils: The use of physical models in treating thermal denaturation equilibria of isolated subsequences of αα-tropomyosin. Biopolymers (Biospectroscopy) 1990, 30, 1231. <http://dx.doi.org/10.1002/bip.360301308>
• Dao-Pin S., Baase W. A., Matthews B. W.: A mutant T4 lysozyme (Val 131 → Ala) designed to increase thermostability by the reduction of strain within an α-helix. Proteins 1990, 7, 198. <http://dx.doi.org/10.1002/prot.340070208>
• Altmann Karl-Heinz, Mutter Manfred: A general strategy for the De novo design of proteins���Template assembled synthetic proteins. International Journal of Biochemistry 1990, 22, 947. <http://dx.doi.org/10.1016/0020-711X(90)90200-M>
• Fairman Robert, Shoemaker Kevin R., York Eunice J., Stewart John M., Baldwin Robert L.: The Glu 2− ⋯ Arg 10+ side-chain interaction in the C-peptide helix of ribonuclease A. biophys chem 1990, 37, 107. <http://dx.doi.org/10.1016/0301-4622(90)88012-H>
• Bradley Erin K., Thomason John F., Cohen Fred E., Kosen Phyllis Anne, Kuntz Irwin D.: Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance. Journal of Molecular Biology 1990, 215, 607. <http://dx.doi.org/10.1016/S0022-2836(05)80172-X>
• Mutter Manfred, Vuilleumier Stéphane: Ein chemischer Weg zu neuen Proteinen – Templat-assoziierte synthetische Proteine (TASP). Angew Chem 1989, 101, 551. <http://dx.doi.org/10.1002/ange.19891010504>
• Mutter Manfred, Vuilleumier Stéphane: A Chemical Approach to Protein Design—Template-Assembled Synthetic Proteins (TASP). Angew Chem Int Ed Engl 1989, 28, 535. <http://dx.doi.org/10.1002/anie.198905353>
• Holtzer Alfred: The effect of sequence-specific interactions on the stability of the α-helix in synthetic tropomyosin-analogue peptides. Biopolymers (Biospectroscopy) 1989, 28, 901. <http://dx.doi.org/10.1002/bip.360280408>
• Vásquez Max, Scheraga Harold A.: Effect of sequence-specific interactions on the stability of helical conformations in polypeptides. Biopolymers (Biospectroscopy) 1988, 27, 41. <http://dx.doi.org/10.1002/bip.360270104>
• Holtzer Alfred, Skolnick Jeffrey: Application of the augmented theory of α-helix-to-random-coil transitions of two-chain, coiled coils to extant data on synthetic, tropomyosin-analog peptides. Biopolymers (Biospectroscopy) 1988, 27, 87. <http://dx.doi.org/10.1002/bip.360270107>
• Kemp D.S., Curran Timothy P.: (2S,5S,8S,11S)-1-Acetyl-1,4-diaza-3-keto-5-carboxy-10-thia-tricyclo-[2.8.04,8]-tridecane, 1 synthesis of prolyl-proline-derived, peptide-functionalized templates for α-helix formation. Tetrahetron Lett 1988, 29, 4931. <http://dx.doi.org/10.1016/S0040-4039(00)80644-9>
• Vasquez Max, Pincus Matthew R., Scheraga Harold A.: Helix-coil transition theory including long-range electrostatic interactions: Application to globular proteins. Biopolymers (Biospectroscopy) 1987, 26, 351. <http://dx.doi.org/10.1002/bip.360260305>
• Vasquez Max, Pincus Matthew R., Scheraga Harold A.: Correlation between computed conformational properties of cytochromec peptides and their antigenicity in a T-lymphocyte proliferation assay. Biopolymers (Biospectroscopy) 1987, 26, 373. <http://dx.doi.org/10.1002/bip.360260306>
• Auer Henry E., Miller-Auer Helene: Dynamics of the disordered-β transition in poly(L-tyrosine) determined by stopped-flow spectrometry. Biopolymers (Biospectroscopy) 1986, 25, 1607. <http://dx.doi.org/10.1002/bip.360250904>
• Eisenberg David, Wilcox William, Eshita Steven M., Pryciak Peter M., Ho Siew Peng, Degrado William F.: The design, synthesis, and crystallization of an alpha-helical peptide. Proteins 1986, 1, 16. <http://dx.doi.org/10.1002/prot.340010105>
• Hecht Michael H., Sturtevant Julian M., Sauer Robert T.: Stabilization of λ repressor against thermal denaturation by site-directed Gly→Ala changes in α-helix 3. Proteins 1986, 1, 43. <http://dx.doi.org/10.1002/prot.340010108>
• Kricheldorf Hans R., Müller Detlef, Hull William E.: Secondary structure of peptides: 19. Primary/secondary structure relationships of leucine/valine copolypeptides prepared from α-amino acid N-carboxyanhydrides. Intern J Biol Macromol 1986, 8, 20. <http://dx.doi.org/10.1016/0141-8130(86)90067-X>
• Hecht Michael H., Hehir Kathleen M., Nelson Hillary C. M., Sturtevant Julian M., Sauer Robert T.: Increasing and decreasing protein stability: Effects of revertant substitutions on the thermal denaturation of phage λ repressor. J Cell Biochem 1985, 29, 217. <http://dx.doi.org/10.1002/jcb.240290306>
• Hecht Michael H., Sauer Robert T.: Phage lambda repressor revertants. Journal of Molecular Biology 1985, 186, 53. <http://dx.doi.org/10.1016/0022-2836(85)90256-6>
• Beachy Philip A., Helfand Stephen L., Hogness David S.: Segmental distribution of bithorax complex proteins during Drosophila development. Appl Opt 1985, 313, 545. <http://dx.doi.org/10.1038/313545a0>
• Scheraga Harold A.: Protein structure and function, from a colloidal to a molecular view. Carlsberg Res Commun 1984, 49, 1. <http://dx.doi.org/10.1007/BF02913964>
• Rico M., Gallego E., Santoro J., Bermejo F.J., Nieto J.L., Herranz J.: On the fundamental role of the glu 2−…Arg 10+ salt bridge in the folding of isolated ribonuclease a S-peptide. BIOPHYS BIOCHEM RES COMMUN 1984, 123, 757. <http://dx.doi.org/10.1016/0006-291X(84)90294-8>
• Kricheldorf Hans R., Hull William E.: Secondary structure of peptidese: 13. 15N and 13C n.m.r. spectroscopic investigation of the helix stability of poly(l-alanine) in acidic solutions. Intern J Biol Macromol 1984, 6, 81. <http://dx.doi.org/10.1016/0141-8130(84)90068-0>
• Kim Peter S., Baldwin Robert L.: A helix stop signal in the isolated S-peptide of ribonuclease A. Appl Opt 1984, 307, 329. <http://dx.doi.org/10.1038/307329a0>
• Kuwajima Kunihiro, Kim Peter S., Baldwin Robert L.: Strategy for trapping intermediates in the folding of ribonuclease and for using1H-NMR to determine their structures. Biopolymers (Biospectroscopy) 1983, 22, 59. <http://dx.doi.org/10.1002/bip.360220111>
• Denton J. B., Powers S. P., Zweifel B. O., Scheraga H. A.: Helix-coil stability constants for the naturally occurring amino acids in water. XXI. Glutamine parameters from random poly(hydroxypropylglutamine-co-L-glutamine) and poly(hydroxybutylglutamine-co-L-glutamine). Biopolymers (Biospectroscopy) 1982, 21, 51. <http://dx.doi.org/10.1002/bip.360210106>
• Bierzynski Andrzej, Baldwin Robert L.: Local secondary structure in ribonuclease A denatured by guanidine · HCl near 1 °C. Journal of Molecular Biology 1982, 162, 173. <http://dx.doi.org/10.1016/0022-2836(82)90167-X>
• Kim Peter S., Bierzynski Andrzej, Baldwin Robert L.: A competing salt-bridge suppresses helix formation by the isolated C-peptide carboxylate of ribonuclease A. Journal of Molecular Biology 1982, 162, 187. <http://dx.doi.org/10.1016/0022-2836(82)90168-1>
• Van Kazuo, Teramoto Akio: Sequential polypeptides: 5. Statistical mechanical analysis of helix-coil transition in sequential polypeptides. Intern J Biol Macromol 1982, 4, 32. <http://dx.doi.org/10.1016/0141-8130(82)90007-1>
• Kubota Yasushi, Nishikawa Ken, Takahashi Sho, Ooi Tatsuo, Miot Francoise, Erneux Christophe: Correspondence of homologies in amino acid sequence and tertiary structure of protein molecules. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1982, 701, 242. <http://dx.doi.org/10.1016/0167-4838(82)90120-0>
• Scheraga Harold A.: Phase transitions in synthetic polymers of amino acids, and their relation to protein folding. GFER 1980, 30, 157. <http://dx.doi.org/10.1080/00150198008209507>