Energetics of ribonuclease T1 structure.

The energetics of thermal denaturation of two isoforms of ribonuclease T1 (Gln25 and Lys25) in various solvents have been studied by differential scanning calorimetry. It has been shown that the thermal transition of both forms of RNase T1 is strongly affected by slow kinetics, which cause an apparent deviation of the transition from a simple two-state model. By decreasing the heating rate or increasing the transition temperature, the denaturation of RNase approaches an equilibrium two-state transition. This permits determination of the thermodynamic parameters characterizing unfolding of the native structure. These thermodynamic parameters were correlated with the structural features of protein. Analysis of different contributions to the stability of RNase T1 shows that van der Waals interactions and hydrogen bonding are the major contributors to the conformational stability of the protein.

[1]  K. Takahashi,et al.  The structure and function of ribonuclease T-1. III. Amino- and carboxyl-terminal sequences of ribonuclease. , 1962 .

[2]  P. Gros,et al.  Lipophilic cations: a group of model substrates for the multidrug-resistance transporter. , 1992, Biochemistry.

[3]  A. Tulinsky,et al.  Three-dimensional structure of Gln25-ribonuclease T1 at 1.84-A resolution: structural variations at the base recognition and catalytic sites. , 1992, Biochemistry.

[4]  C. Pace,et al.  Conformational stability and mechanism of folding of ribonuclease T1. , 1989, The Journal of biological chemistry.

[5]  A. Rashin,et al.  Buried surface area, conformational entropy, and protein stability , 1984, Biopolymers.

[6]  T. Creighton,et al.  The disulphide folding pathway of ribonuclease T1. , 1986, Journal of molecular biology.

[7]  P. Privalov,et al.  Scanning microcalorimetry in studying temperature-induced changes in proteins. , 1986, Methods in enzymology.

[8]  D. Laurents,et al.  pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. , 1990, Biochemistry.

[9]  P. Privalov,et al.  Heat capacity and conformation of proteins in the denatured state. , 1989, Journal of molecular biology.

[10]  C. Pace,et al.  Temperature and guanidine hydrochloride dependence of the structural stability of ribonuclease T1. , 1992, Biochemistry.

[11]  D. Tobias,et al.  The role of packing interactions in stabilizing folded proteins. , 1992, Biochemistry.

[12]  P. Privalov,et al.  Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range , 1990, Biopolymers.

[13]  T. Ooi,et al.  Titration of ribonuclease T1. , 1969, Biochemistry.

[14]  U. Heinemann,et al.  Specific protein-nucleic acid recognition in ribonuclease T1–2′-guanylic acid complex: an X-ray study , 1982, Nature.

[15]  C. Pace,et al.  Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. , 1992, Biochemistry.

[16]  E. Freire,et al.  Statistical mechanical deconvolution of thermal transitions in macromolecules. I. Theory and application to homogeneous systems , 1978 .

[17]  P. Privalov,et al.  A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. , 1974, Journal of molecular biology.

[18]  C. Pace,et al.  Thermodynamics of ribonuclease T1 denaturation. , 1992, Biochemistry.

[19]  J. Sturtevant Biochemical Applications of Differential Scanning Calorimetry , 1987 .

[20]  Pace Cn,et al.  Ribonuclease T1 is stabilized by cation and anion binding. , 1988 .

[21]  G. Mosser,et al.  A 9 A two-dimensional projected structure of cholera toxin B-subunit-GM1 complexes determined by electron crystallography. , 1992, Journal of molecular biology.

[22]  L. Jaenicke A rapid micromethod for the determination of nitrogen and phosphate in biological material. , 1974, Analytical biochemistry.

[23]  U. Hahn,et al.  Stability of recombinant Lys25-ribonuclease T1. , 1990, Biochemistry.

[24]  P. Privalov,et al.  Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect. , 1990, Journal of molecular biology.

[25]  C. Pace,et al.  Contribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58----Ala. , 1990, Biochemistry.

[26]  A M Lesk,et al.  Interior and surface of monomeric proteins. , 1987, Journal of molecular biology.

[27]  D. Fessas,et al.  Thermal denaturation of ribonuclease T1 a DSC study , 1992 .

[28]  P. Privalov,et al.  Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding. , 1992, Journal of molecular biology.

[29]  A. Winder,et al.  Correction of light‐scattering errors in spectrophotometric protein determinations , 1971, Biopolymers.

[30]  C. Pace,et al.  Conformational Stability and Activity of Ribonuclease T1 and Mutants , 1989 .

[31]  S. Moore,et al.  13 Ribonuclease T1 , 1982 .

[32]  D A Yphantis,et al.  STUDIES OF SELF‐ASSOCIATING SYSTEMS BY EQUILIBRIUM ULTRACENTRIFUGATION * , 1969, Annals of the New York Academy of Sciences.

[33]  O. Ptitsyn,et al.  Determination of stability of the DNA double helix in an aqueous medium , 1969 .

[34]  P. Privalov,et al.  Three generations of scanning microcalorimeters for liquids , 1989 .

[35]  P. Privalov,et al.  Contribution of hydration to protein folding thermodynamics. I. The enthalpy of hydration. , 1993, Journal of molecular biology.

[36]  T. Kiefhaber,et al.  Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models. , 1992, Journal of molecular biology.

[37]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.

[38]  D. Laurents,et al.  Purification of recombinant ribonuclease T1 expressed in Escherichia coli. , 1990, Journal of biochemical and biophysical methods.

[39]  J. Lepock,et al.  Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. , 1992, Biochemistry.

[40]  P. Privalov,et al.  Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration. , 1993, Journal of molecular biology.

[41]  I. Shimada,et al.  Nuclear magnetic resonance study on the microenvironments of histidine residues of ribonuclease T1 and carboxymethylated ribonuclease T1. , 1981, Journal of biochemistry.

[42]  G. Ellman,et al.  Tissue sulfhydryl groups. , 1959, Archives of biochemistry and biophysics.

[43]  P. Privalov,et al.  Cold denaturation of myoglobin. , 1986, Journal of molecular biology.

[44]  E. Freire,et al.  Fluorescence and calorimetric studies of phase transitions in phosphatidylcholine multilayers: kinetics of the pretransition. , 1978, Biochemistry.

[45]  P. Privalov,et al.  Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects. , 1990, Journal of molecular biology.

[46]  T. Kiefhaber,et al.  Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1. , 1992, Journal of molecular biology.

[47]  K. Dill,et al.  Hydrogen bonding in globular proteins. , 1992, Journal of molecular biology.

[48]  Clare Woodward,et al.  Thermodynamics of bpti folding , 1993, Protein science : a publication of the Protein Society.

[49]  Thomas E. Creighton,et al.  Stability of folded conformations , 1991 .