Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl‐prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18)

Refolding of b*C40A/C82A/P27A is comprised of several kinetically detectable folding phases. The slowest phase in refolding originates from trans → cis isomerization of the Tyr47–Pro48 peptide bond being in cis conformation in the native state. This refolding phase can be accelerated by the peptidyl‐prolyl cis/trans isomerase human cytosolic cyclophilin (Cyp18) with a kcat/KM of 254, 000 M–1 s–1. The fast refolding phase is not influenced by the enzyme.

[1]  Bengt Nölting,et al.  Mechanism of protein folding , 2000, Proteins.

[2]  U. Reimer,et al.  Intramolecular assistance of cis/trans isomerization of the histidine-proline moiety. , 1997, Biochemistry.

[3]  J. Udgaonkar,et al.  Thermodynamics of the complex protein unfolding reaction of barstar. , 1997, Biochemistry.

[4]  D. Kern,et al.  Rotational Barriers of cis/trans Isomerization of Proline Analogues and Their Catalysis by Cyclophilin§ , 1997 .

[5]  J. Udgaonkar,et al.  Folding of tryptophan mutants of barstar: evidence for an initial hydrophobic collapse on the folding pathway. , 1997, Biochemistry.

[6]  G Schreiber,et al.  The role of Glu73 of barnase in catalysis and the binding of barstar. , 1997, Journal of molecular biology.

[7]  G Schreiber,et al.  The folding pathway of a protein at high resolution from microseconds to seconds. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[8]  J. Udgaonkar,et al.  Initial loss of secondary structure in the unfolding of barstar , 1996, Nature Structural Biology.

[9]  A. Fersht,et al.  Submillisecond events in protein folding. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[10]  J. Udgaonkar,et al.  Initial hydrophobic collapse in the folding of barstar , 1995, Nature.

[11]  D. Kern,et al.  Kinetic analysis of cyclophilin-catalyzed prolyl cis/trans isomerization by dynamic NMR spectroscopy. , 1995, Biochemistry.

[12]  A. Fersht,et al.  Characterization of in vitro oxidized barstar , 1995, FEBS letters.

[13]  P. Privalov,et al.  Structural energetics of barstar studied by differential scanning microcalorimetry , 1995, Protein science : a publication of the Protein Society.

[14]  A. Fersht,et al.  A calorimetric study of the thermal stability of barstar and its interaction with barnase. , 1995, Biochemistry.

[15]  J. Udgaonkar,et al.  The folding mechanism of barstar: evidence for multiple pathways and multiple intermediates. , 1995, Journal of molecular biology.

[16]  G. Fischer Peptidyl‐Prolyl cis/trans Isomerases and Their Effectors , 1994 .

[17]  H. Dyson,et al.  Stabilization of a type VI turn in a family of linear peptides in water solution. , 1994, Journal of molecular biology.

[18]  J. Udgaonkar,et al.  Crystallization and molecular packing analysis of barstar crystals. , 1994, Journal of Molecular Biology.

[19]  J. Udgaonkar,et al.  Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone , 1994, Protein science : a publication of the Protein Society.

[20]  G. Fischer,et al.  Peptidyl-prolyl cis/trans isomerases and their effectors , 1994 .

[21]  A. Fersht,et al.  Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution. , 1994, Biochemistry.

[22]  C. Kim,et al.  Engineered tyrosine residues serve as the local probes to detect a kinetic intermediate in the folding of ribose-binding protein. , 1994, Journal of Molecular Biology.

[23]  M. Eftink The use of fluorescence methods to monitor unfolding transitions in proteins. , 1994, Biophysical journal.

[24]  V. Hsu,et al.  Thermodynamics of cyclophilin catalyzed peptidyl‐prolyl isomerization by nmr spectroscopy , 1994, Biopolymers.

[25]  B. Nall,et al.  Characterization of folding intermediates using prolyl isomerase. , 1994, Biochemistry.

[26]  M. Walkinshaw,et al.  X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution. , 1993, Journal of molecular biology.

[27]  I. Weissman,et al.  Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[28]  V. Guillet,et al.  Crystallization and prelilminary X‐ray investigation of barster, the intracellular inhibitor of barnase , 1993 .

[29]  J. Thornton,et al.  Conformational analysis of protein structures derived from NMR data , 1993, Proteins.

[30]  A. Fersht,et al.  The refolding of cis- and trans-peptidylprolyl isomers of barstar. , 1993, Biochemistry.

[31]  D. Kern,et al.  The cis/trans interconversion of the calcium regulating hormone calcitonin is catalyzed by cyclophilin , 1993, FEBS letters.

[32]  A. Fersht,et al.  Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. , 1993, Biochemistry.

[33]  L Serrano,et al.  The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure. , 1992, Journal of molecular biology.

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

[35]  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.

[36]  P. Kraulis A program to produce both detailed and schematic plots of protein structures , 1991 .

[37]  J. Thornton,et al.  Influence of proline residues on protein conformation. , 1991, Journal of molecular biology.

[38]  Andreas Matouschek,et al.  Transient folding intermediates characterized by protein engineering , 1990, Nature.

[39]  F. Schmid,et al.  The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell. , 1990, Biochemistry.

[40]  R. Stein,et al.  Mechanistic studies of peptidyl prolyl cis-trans isomerase: evidence for catalysis by distortion. , 1990, Biochemistry.

[41]  R. Hartley,et al.  Barnase and barstar: two small proteins to fold and fit together. , 1989, Trends in biochemical sciences.

[42]  P. V. von Hippel,et al.  Calculation of protein extinction coefficients from amino acid sequence data. , 1989, Analytical biochemistry.

[43]  A. Fersht,et al.  Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis. , 1989, Biochemistry.

[44]  D. W. Bolen,et al.  Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. , 1988, Biochemistry.

[45]  D. W. Bolen,et al.  Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle. , 1988, Biochemistry.

[46]  R. Hartley,et al.  Barnase and barstar. Expression of its cloned inhibitor permits expression of a cloned ribonuclease. , 1988, Journal of molecular biology.

[47]  F. Schmid,et al.  Catalysis of protein folding by prolyl isomerase , 1987, Nature.

[48]  F. Schmid Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates. , 1983, Biochemistry.

[49]  K. Wüthrich,et al.  Nmr studies of the rates of proline cis–trans isomerization in oligopeptides , 1981 .

[50]  R. L. Baldwin,et al.  Refolding behavior of a kinetic intermediate observed in the low pH unfolding of ribonuclease A. , 1979, Biochemistry.

[51]  R. L. Baldwin,et al.  Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[52]  K. Wüthrich,et al.  Nmr studies of the molecular conformations in the linear oligopeptides H‐(L‐Ala)n‐L‐Pro‐OH , 1976, Biopolymers.

[53]  K. Wüthrich,et al.  The X‐Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides , 1976, Biopolymers.

[54]  H. Halvorson,et al.  Consideration of the Possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. , 1975, Biochemistry.

[55]  F. Schmid,et al.  Prolyl isomerases: role in protein folding. , 1993, Advances in protein chemistry.

[56]  R. Stein Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization. , 1993, Advances in protein chemistry.

[57]  F. Schmid,et al.  Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. , 1993, Annual review of biophysics and biomolecular structure.

[58]  F. Schmid Kinetics of unfolding and refolding of single-domain proteins , 1992 .

[59]  A. Fersht,et al.  Protein engineering in analysis of protein folding pathways and stability. , 1991, Methods in enzymology.

[60]  G Blomqvist,et al.  Kinetic analysis. , 1991, Wiener klinische Wochenschrift.

[61]  P. S. Kim,et al.  Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding. , 1982, Annual review of biochemistry.