Pure and Applied Chemistry

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• Goldberg Robert N.: Standards in biothermodynamics. Perspectives in Science 2014. <http://dx.doi.org/10.1016/j.pisc.2014.02.001>
• Dukhopelnikov E. V., Bereznyak E. G., Khrebtova A. S., Lantushenko A. O., Zinchenko A. V.: Determination of ligand to DNA binding parameters from two-dimensional DSC curves. J Therm Anal Calorim 2013, 111, 1817. <http://dx.doi.org/10.1007/s10973-012-2561-6>
• Senthilkumar Namasivayam, Kurinjimalar Chidambaram, Thangam Ramar, Suresh Veeraperumal, Kavitha Ganapathy, Gunasekaran Palani, Rengasamy Ramasamy: Further studies and biological activities of macromolecular protein R-Phycoerythrin from Portieria hornemannii. International Journal of Biological Macromolecules 2013, 62, 107. <http://dx.doi.org/10.1016/j.ijbiomac.2013.08.004>
• Lund Henrik, Kaasgaard Svend Gunnar, Skagerlind Peter, Jorgensen Lene, Jorgensen Christian Isak, Weert Marco: Correlation Between Enzyme Activity and Stability of a Protease, an Alpha-Amylase and a Lipase in a Simplified Liquid Laundry Detergent System, Determined by Differential Scanning Calorimetry. J Surfact Deterg 2012, 15, 9. <http://dx.doi.org/10.1007/s11743-011-1272-5>
• Lund Henrik, Kaasgaard Svend Gunnar, Skagerlind Peter, Jorgensen Lene, Jørgensen Christian Isak, Weert Marco: Protease and Amylase Stability in the Presence of Chelators Used in Laundry Detergent Applications: Correlation Between Chelator Properties and Enzyme Stability in Liquid Detergents. J Surfact Deterg 2012, 15, 265. <http://dx.doi.org/10.1007/s11743-011-1318-8>
• Antonov Yurij A., Zhuravleva Irina L.: Macromolecular complexes of BSA with gelatin. International Journal of Biological Macromolecules 2012, 51, 319. <http://dx.doi.org/10.1016/j.ijbiomac.2012.05.012>
• Svanidze Anna V., Huth Heiko, Lushnikov Sergey G., Schick Christoph: Study of phase transition in tetragonal lysozyme crystals by AC-nanocalorimetry. Thermochimica Acta 2012, 544, 33. <http://dx.doi.org/10.1016/j.tca.2012.06.013>
• Garbett Nichola C, Chaires Jonathan B: Thermodynamic studies for drug design and screening. Expert Opin Drug Disc 2012, 7, 299. <http://dx.doi.org/10.1517/17460441.2012.666235>
• Frenkel Michael, Chirico Robert D., Diky Vladimir, Brown Paul L., Dymond John H., Goldberg Robert N., Goodwin Anthony R. H., Heerklotz Heiko, Königsberger Erich, Ladbury John E.: Extension of ThermoML: The IUPAC standard for thermodynamic data communications (IUPAC Recommendations 2011). PureAppl Chem 2011, 1. <http://dx.doi.org/10.1351/PAC-REC-11-05-01>
• Pavišić Renata, Dodig Ivana, Horvatić Anita, Mijić Lucija, Sedić Mirela, Linarić Maša Rajić, Sovulj Ita Gruić, Preočanin Tajana, Krajačić Mirjana Bukvić, Cindrić Mario: Differences between reversible (self-association) and irreversible aggregation of rHuG-CSF in carbohydrate and polyol formulations. Eur J Pharma Biopharm 2010, 76, 357. <http://dx.doi.org/10.1016/j.ejpb.2010.09.006>
• Kavitha M., Swamy Musti J.: Spectroscopic and differential scanning calorimetric studies on the unfolding of Trichosanthes dioica seed lectin. Similar modes of thermal and chemical denaturation. Glycoconjugate J 2009, 26, 1075. <http://dx.doi.org/10.1007/s10719-009-9228-y>
• Seki Shinsuke, Kleinhans F.W., Mazur Peter: Intracellular ice formation in yeast cells vs. cooling rate: Predictions from modeling vs. experimental observations by differential scanning calorimetry. Crybiology 2009, 58, 157. <http://dx.doi.org/10.1016/j.cryobiol.2008.11.011>
• Goyal Monu Kumari, Roy Ipsita, Banerjee Uttam Chand, Sharma Vikas Kumar, Bansal Arvind Kumar: Role of benzyl alcohol in the prevention of heat-induced aggregation and inactivation of hen egg white lysozyme. Eur J Pharma Biopharm 2009, 71, 367. <http://dx.doi.org/10.1016/j.ejpb.2008.09.012>
• Antonov Y.A., Sato Takahiro: Macromolecular complexes of the main storage protein of Vicia faba seeds with sulfated polysaccharide. Food Hydrocoll 2009, 23, 996. <http://dx.doi.org/10.1016/j.foodhyd.2008.07.012>
• Bereznyak E. G., Gladkovskaya N. A., Khrebtova A. S., Dukhopelnikov E. V., Zinchenko A. V.: Peculiarities of DNA-proflavine binding under different concentration ratios. Biophysics 2009, 54, 574. <http://dx.doi.org/10.1134/S0006350909050030>
• Giancola Concetta: A convenient tool for studying the stability of proteins and nucleic acids. J Therm Anal Calorim 2008, 91, 79. <http://dx.doi.org/10.1007/s10973-007-8436-6>
• Chaires Jonathan B.: Calorimetry and Thermodynamics in Drug Design. Annu Rev Biophys 2008, 37, 135. <http://dx.doi.org/10.1146/annurev.biophys.36.040306.132812>
• Altermark Bjørn, Niiranen Laila, Willassen Nils P., Smalås Arne O., Moe Elin: Comparative studies of endonuclease I from cold-adapted Vibrio salmonicida and mesophilic Vibrio cholerae : Endonuclease I from V. salmonicida and V. cholerae. FEBS J 2007, 274, 252. <http://dx.doi.org/10.1111/j.1742-4658.2006.05580.x>
• Zevatskii Yu. E., Samoilov D. V.: Empirical method for calculation of thermodynamic potentials of organic substances. Russ J Appl Chem 2007, 80, 230. <http://dx.doi.org/10.1134/S1070427207020127>
• Noronha Melinda, Lima Jo�o C., Paci Emanuele, Santos Helena, Ma�anita Ant�nio L.: Tracking Local Conformational Changes of Ribonuclease A Using Picosecond Time-Resolved Fluorescence of the Six Tyrosine Residues. Biophysical Journal 2007, 92, 4401. <http://dx.doi.org/10.1529/biophysj.106.093625>
• Zielenkiewicz W, Swierzewski R, Attanasio F, Rialdi G: Thermochemical, volumetric and spectroscopic properties of lysozyme–poly(ethylene) glycol system. J Therm Anal Calorim 2006, 83, 587. <http://dx.doi.org/10.1007/s10973-005-7417-x>
• Attanasio F., Rialdi G., Swierzewski R., Zielenkiewicz W.: Pressure perturbation calorimetry of poly(ethylene) glycol solutions in water. J Therm Anal Calorim 2006, 83, 637. <http://dx.doi.org/10.1007/s10973-005-7426-9>
• Kleinhans F.W., Guenther J.F., Roberts D.M., Mazur Peter: Analysis of intracellular ice nucleation in Xenopus oocytes by differential scanning calorimetry. Crybiology 2006, 52, 128. <http://dx.doi.org/10.1016/j.cryobiol.2005.10.008>
• Almeida Nara L., Oliveira Cristiano L.P., Torriani Iris L., Loh Watson: Calorimetric and structural investigation of the interaction of lysozyme and bovine serum albumin with poly(ethylene oxide) and its copolymers. Colloids Surface B 2004, 38, 67. <http://dx.doi.org/10.1016/j.colsurfb.2004.08.004>
• Noronha Melinda, Lima Jo�o C., Bastos Margarida, Santos Helena, Ma�anita Ant�nio L.: Unfolding of Ubiquitin Studied by Picosecond Time-Resolved Fluorescence of the Tyrosine Residue. Biophysical Journal 2004, 87, 2609. <http://dx.doi.org/10.1529/biophysj.104.046466>
• Sarai Akinori, Gromiha M. Michael, An Jianghong, Prabakaran Ponraj, Selvaraj Samuel, Kono Hidetoshi, Oobatake Motohisa, Uedaira Hatsuho: Thermodynamic databases for proteins and protein-nucleic acid interactions. Biopolymers (Biospectroscopy) 2001, 61, 121. <http://dx.doi.org/10.1002/1097-0282(2002)61:2<121::AID-BIP10077>3.0.CO;2-1>