@article {4236,
	title = {Stability and oligosaccharide binding of the N1 cellulose-binding domain of Cellulomonas fimi endoglucanase CenC},
	journal = {Biochemistry},
	volume = {37},
	number = {10},
	year = {1998},
	note = {ISI Document Delivery No.: ZC900Times Cited: 16Cited Reference Count: 75},
	month = {Mar},
	pages = {3529-3537},
	type = {Article},
	abstract = {Differential scanning calorimetry has been used to study the thermal stability and oligosaccharide-binding thermodynamics of the N-terminal cellulose-binding domain of Cellulomonas fimi beta-1,4-glucanase CenC (CBDN1) CBDN1 has a relatively low maximum stability (Delta G(max) = 33 kJ/mol = 216 J/residue at 1 degrees C and pH 6.1) compared to other small single-domain globular proteins. The unfolding is fully reversible between pH 5.5 and 9 and in accordance with the two-state equilibrium model between pH 5.5 and 11. When the single disulfide bond in CBDN1 is reduced, the protein remains unfolded at all conditions, as judged by NMR spectroscopy. This indicates that the intramolecular cross-link makes a major contribution to the stability of CBDN1. The measured heat capacity change of unfolding (Delta C-p = 7.5 kJ mol(-1) K-1) agrees well with that calculated from the predicted changes in the solvent accessible nonpolar and polar surface areas upon unfolding. Extrapolation of the specific enthalpy and entropy of unfolding to their respective convergence temperature indicates that per residue unfolding energies for CBDN1, an isolated domain, are in accordance with those found by Privalov (1) for many single-domain globular proteins. DSC thermograms of the unfolding of CBDN1 in the presence of various concentrations of cellopentaose were fit to a thermodynamic model describing the linkage between protein-ligand binding and protein unfolding. A global two-dimensional minimization routine is used to regress the binding enthalpy, binding constant, and unfolding thermodynamics for the CBDN1-cellopentaose system. Extrapolated binding constants are in quantitative agreement with those determined by isothermal titration calorimetry at 35 degrees C.},
	keywords = {ASPERGILLUS-NIGER, BRIDGES, differential scanning calorimetry, Disulfide, ESCHERICHIA-COLI, GLOBULAR-PROTEINS, INHIBITOR BINDING, LIGAND-BINDING, PROTEIN-FOLDING THERMODYNAMICS, THERMAL-DENATURATION, TITRATION CALORIMETRY},
	isbn = {0006-2960},
	url = {<Go to ISI>://000072630300034},
	author = {Creagh, A. L. and Koska, J. and Johnson, P. E. and Tomme, P. and Joshi, M. D. and McIntosh, L. P. and Kilburn, D. G. and Haynes, C. A.}
}
@article {4155,
	title = {Intermolecular interactions of lysozyme and small alcohols: A calorimetric investigation},
	journal = {Journal of Physical Chemistry B},
	volume = {101},
	number = {29},
	year = {1997},
	note = {ISI Document Delivery No.: XM058Times Cited: 23Cited Reference Count: 34},
	month = {Jul},
	pages = {5755-5758},
	type = {Article},
	abstract = {Isothermal titration calorimetry was used to measure transfer enthalpies of hen egg white lysozyme from water to aqueous solutions of methanol, ethanol, 1-propanol, glycerol, and 2,2,2-trifluoroethanol. Excess partial molar enthalpies of lysozyme at infinite dilution in the alcoholic solvents, H-infinity(L)E, were calculated, and the dependence of H-infinity(L)E on the concentration of the alcohol, was utilized to elucidate the enthalpy of alcohol-protein interactions. Results show that, at low alcohol concentrations, alcohol-protein interactions are unfavorable in terms of enthalpy (endothermic), while at higher concentrations they are favorable (exothermic). The change from endothermic to exothermic interactions happened sharply over a narrow alcohol concentration interval, and was found to occur concurrently with denaturation of the protein in some but not all cases. Comparison of the present results with previous investigations of simple binary and ternary aqueous solutions suggests that the change of sign of the interaction enthalpy is related to the water-water hydrogen bonding properties in the alcohol mixtures. It is argued that modifications by the alcohol of the percolated hydrogen bond network govern the enthalpy of alcohol-lysozyme interactions in the most water-rich samples. This suggests that occupancy by the alcohol of a binding site on the surface of the protein may not be necessary for the alcohol to affect the properties of the protein. At higher alcohol concentrations the observed interaction enthalpies are dominated by direct ({\textquoteright}{\textquoteright}intrinsic{\textquoteright}{\textquoteright}) effects of protein-alcohol interactions, which are exothermic.},
	keywords = {25-DEGREES-C, ENERGIES, GLOBULAR-PROTEINS, INDUCED REVERSIBLE DENATURATION, MIXTURES, MONOHYDRIC ALCOHOLS, STABILIZATION, THERMODYNAMIC INVESTIGATIONS, TRIFLUOROETHANOL, VAPOR-PRESSURES, WATER},
	isbn = {1089-5647},
	url = {<Go to ISI>://A1997XM05800021},
	author = {Westh, P. and Koga,Yoshikata}
}
@article {3763,
	title = {Driving forces for DNA adsorption to silica in perchlorate solutions},
	journal = {Journal of Colloid and Interface Science},
	volume = {181},
	number = {2},
	year = {1996},
	note = {ISI Document Delivery No.: UZ536Times Cited: 112Cited Reference Count: 43},
	month = {Aug},
	pages = {635-644},
	type = {Article},
	abstract = {The adsorption of both plasmid and chromosomal duplex DNA to silica is investigated with the aim of determining the dominant forces involved in the binding reaction. Changes in the initial slopes and plateau values of adsorption isotherms for DNA on microcrystalline silica particles are used to establish the sensitivity of the binding reaction to ionic strength, temperature and pH, and DNA size and conformation. Binding is driven by an increase in entropy, with little or no enthalpic contribution. Adsorption isotherm results indicate that three effects, namely: (i) shielded intermolecular electrostatic forces, (ii) dehydration of the DNA and silica surfaces, and (iii) intermolecular hydrogen bond formation in the DNA-silica contact layer, make the dominant contributions to the overall driving force for adsorption. (C) 1996 Academic Press, Inc.},
	keywords = {adsorption isotherms, ARRAYS, CHIPS, CONFORMATION, DNA, DNA adsorption, DNA binding, DNA PURIFICATION, DNA-silica interactions, ELECTROPHORESIS, GLOBULAR-PROTEINS, PLASMID DNA, PURIFICATION, SURFACES, TRANSITION},
	isbn = {0021-9797},
	url = {<Go to ISI>://A1996UZ53600031},
	author = {Melzak, K. A. and Sherwood, C. S. and Turner, R. F. B. and Haynes, C. A.}
}
@article {2925,
	title = {CIRCULAR-DICHROISM ANALYSIS OF A SYNTHETIC PEPTIDE CORRESPONDING TO THE ALPHA,ALPHA-CORNER MOTIF OF HEMOGLOBIN},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {196},
	number = {1},
	year = {1993},
	note = {ISI Document Delivery No.: MC105Times Cited: 1Cited Reference Count: 16},
	month = {Oct},
	pages = {435-439},
	type = {Article},
	keywords = {ALPHA-HELIX, GLOBULAR-PROTEINS, INTERMEDIATE, POLYPEPTIDE-CHAIN, SECONDARY STRUCTURE, STABILITY},
	isbn = {0006-291X},
	url = {<Go to ISI>://A1993MC10500062},
	author = {Tsai, F. C. S. and Sherman, J. C.}
}
