Counteracting effects of thiocyanate and sucrose on chymotrypsinogen secondary structure and aggregation during freezing, drying, and rehydration.

[1]  E. Gabellieri,et al.  Proteins in frozen solutions: evidence of ice-induced partial unfolding. , 1996, Biophysical journal.

[2]  M. Manning,et al.  Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states. , 1996, Journal of pharmaceutical sciences.

[3]  D. W. Bolen,et al.  The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. , 1995, Biochemistry.

[4]  S. Allison,et al.  Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. , 1995, Journal of pharmaceutical sciences.

[5]  T. Arakawa,et al.  Structure of Proteins in Lyophilized Formulations Using Fourier Transform Infrared Spectroscopy. , 1995 .

[6]  T. Lin,et al.  Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein. , 1994, Biochemistry.

[7]  W. Caughey,et al.  Infrared methods for study of hemoglobin reactions and structures. , 1994, Methods in enzymology.

[8]  T. Arakawa,et al.  Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. , 1993, Biophysical journal.

[9]  S J Prestrelski,et al.  Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. I. Enzyme activity and calorimetric studies. , 1993, Archives of biochemistry and biophysics.

[10]  S J Prestrelski,et al.  Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. II. Structural studies using infrared spectroscopy. , 1993, Archives of biochemistry and biophysics.

[11]  H. Mantsch,et al.  Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment. , 1993, Biochemistry.

[12]  S. N. Timasheff.  Water as ligand: preferential binding and exclusion of denaturants in protein unfolding. , 1992, Biochemistry.

[13]  B. Caughey,et al.  Secondary structure of the pentraxin female protein in water determined by infrared spectroscopy: effects of calcium and phosphorylcholine. , 1992, Biochemistry.

[14]  B. Chang,et al.  Use of subambient thermal analysis to optimize protein lyophilization , 1992 .

[15]  H. Mantsch,et al.  Aggregation of chymotrypsinogen: portrait by infrared spectroscopy. , 1992, Biochimica et biophysica acta.

[16]  W. Caughey,et al.  Protein secondary structures in water from second-derivative amide I infrared spectra. , 1990, Biochemistry.

[17]  J. Carpenter,et al.  An infrared spectroscopic study of the interactions of carbohydrates with dried proteins. , 1989, Biochemistry.

[18]  J. Carpenter,et al.  The mechanism of cryoprotection of proteins by solutes. , 1988, Cryobiology.

[19]  H. Susi,et al.  Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. , 1986, Methods in enzymology.

[20]  T. Arakawa,et al.  Stabilization of protein structure by sugars. , 1982, Biochemistry.

[21]  T. Arakawa,et al.  Preferential interactions of proteins with salts in concentrated solutions. , 1982, Biochemistry.

[22]  A. Clark,et al.  Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels. , 2009, International journal of peptide and protein research.

[23]  A. Minton.  Excluded volume as a determinant of macromolecular structure and reactivity , 1981 .

[24]  J. Lee,et al.  The stabilization of proteins by sucrose. , 1981, The Journal of biological chemistry.

[25]  N. Kaplan,et al.  EFFECTS OF FREEZING ON ENZYMES. , 1965, Federation proceedings.

[26]  R. Lumry,et al.  THE REVERSIBLE THERMAL DENATURATION OF CHYMOTRYPSINOGEN.1 I. EXPERIMENTAL CHARACTERIZATION , 1963 .

[27]  K. Shikama,et al.  Denaturation of Catalase by Freezing and Thawing , 1961, Nature.

[28]  G. Schwert,et al.  THE REVERSIBLE HEAT DENATURATION OF CHYMOTRYPSINOGEN , 1951, The Journal of general physiology.