Side-chain effects on peptidyl-prolyl cis/trans isomerisation.
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G Fischer | U. Reimer | M. Schutkowski | G. Fischer | M Schutkowski | M Drewello | G. Scherer | M. Drewello | S. Kruber | U Reimer | G Scherer | S Kruber
[1] U. Reimer,et al. Intramolecular assistance of cis/trans isomerization of the histidine-proline moiety. , 1997, Biochemistry.
[2] A. Superti-Furga,et al. Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase. , 1991, The Journal of biological chemistry.
[3] U. Hobohm,et al. Enlarged representative set of protein structures , 1994, Protein science : a publication of the Protein Society.
[4] A. Drake,et al. The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides , 1995, Biopolymers.
[5] S. Meiboom,et al. Nuclear Magnetic Resonance Study of the Protolysis and Ionization of N-Methylacetamide1 , 1959 .
[6] D. Case,et al. Thermodynamics of a reverse turn motif. Solvent effects and side-chain packing. , 1997, Journal of Molecular Biology.
[7] R. Kautz,et al. NMR analysis of staphylococcal nuclease thermal quench refolding kinetics , 1993, Protein science : a publication of the Protein Society.
[8] H. Scheraga,et al. Nature of the unfolded state of ribonuclease A: effect of cis-trans X-Pro peptide bond isomerization. , 1996, Biochemistry.
[9] R. Stein,et al. Mechanistic studies of enzymic and nonenzymic prolyl cis-trans isomerization , 1992 .
[10] I. Campbell,et al. Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[11] R. Stein,et al. Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes. , 1990, Biochemistry.
[12] Roland L. Dunbrack,et al. Cis-Trans Imide Isomerization of the Proline Dipeptide , 1994 .
[13] Richard S. Rosenstein,et al. Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase. , 1992, Biochemistry.
[14] H. Dyson,et al. Stabilization of a type VI turn in a family of linear peptides in water solution. , 1994, Journal of molecular biology.
[15] P. Y. Chou,et al. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. , 1974, Biochemistry.
[16] C. Fierke,et al. Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202-->alanine carbonic anhydrase II variant. , 1993, Biochemistry.
[17] H. Dyson,et al. Three-dimensional structure of a type VI turn in a linear peptide in water solution. Evidence for stacking of aromatic rings as a major stabilizing factor. , 1994, Journal of molecular biology.
[18] F. Schmid,et al. Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding. , 1995, Journal of molecular biology.
[19] K. Wüthrich,et al. Nmr studies of the rates of proline cis–trans isomerization in oligopeptides , 1981 .
[20] T. Creighton,et al. The physical properties of local interactions of tyrosine residues in peptides and unfolded proteins. , 1995, Journal of molecular biology.
[21] L Serrano,et al. Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. , 1997, Journal of molecular biology.
[22] M. Schutkowski,et al. Inhibition of peptidyl-prolyl cis/trans isomerase activity by substrate analog structures: thioxo tetrapeptide-4-nitroanilides. , 1995, Biochemistry.
[23] R. Stein,et al. Mechanistic studies of peptidyl prolyl cis-trans isomerase: evidence for catalysis by distortion. , 1990, Biochemistry.
[24] U. Reimer,et al. Role of phosphorylation in determining the backbone dynamics of the serine/threonine-proline motif and Pin1 substrate recognition. , 1998, Biochemistry.
[25] M. Sternberg,et al. Left-handed polyproline II helices commonly occur in globular proteins. , 1993, Journal of molecular biology.
[26] Greet Vanhoof,et al. Proline motifs in peptides and their biological processing , 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[27] J. Frère,et al. The rate‐limiting step in the folding of the cis‐Pro167Thr mutant of TEM‐1 β‐lactamase is the trans to cis isomerization of a non‐proline peptide bond , 1996, Proteins.
[28] P. Y. Chou,et al. β-turns in proteins☆ , 1977 .
[29] U. Reimer,et al. Conformational state of a 25-mer peptide from the cyclophilin-binding loop of the HIV type 1 capsid protein. , 1997, The Biochemical journal.
[30] F. Schmid,et al. Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. , 1993, Annual review of biophysics and biomolecular structure.
[31] M. Llinás,et al. CHARGE RELAY AT THE PEPTIDE BOND: A PROTON MAGNETIC RESONANCE STUDY OF SOLVATION EFFECTS ON THE AMIDE ELECTRON DENSITY DISTRIBUTION , 1974 .
[32] R. Stein. Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization. , 1993, Advances in protein chemistry.
[33] R. Timpl,et al. Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization. , 1980, European journal of biochemistry.
[34] K. Wüthrich,et al. The X‐Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides , 1976, Biopolymers.
[35] M. Llinás,et al. Solution conformation of the ferrichromes. VI. Charge relay at the peptide bond. Proton magnetic resonance study of solvation effects on the amide electron density distribution , 1975 .
[36] D. Case,et al. Dynamics of a type VI reverse turn in a linear peptide in aqueous solution. , 1997, Folding & design.
[37] A. Fersht,et al. The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2. , 1997, Journal of molecular biology.
[38] T. Lectka,et al. INTRAMOLECULAR CATALYSIS OF AMIDE ISOMERIZATION , 1997 .
[39] F. Schmid,et al. Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique. , 1996, Biochemistry.
[40] R. Wade,et al. Local interactions of aromatic residues in short peptides in aqueous solution: a combined database and energetic analysis. , 1997, Folding & design.
[41] J. Thornton,et al. Influence of proline residues on protein conformation. , 1991, Journal of molecular biology.
[42] P E Wright,et al. Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn. , 1988, Journal of molecular biology.
[43] A. Aubry,et al. .beta.I and .beta.II-turn conformations in model dipeptides with the Pro-Xaa sequences , 1985 .
[44] M. Schutkowski,et al. Evidence for the Absolute Conformational Specificity of the Intestinal H+/Peptide Symporter, PEPT1* , 1998, The Journal of Biological Chemistry.
[45] I. Z. Steinberg,et al. The Configurational Changes of Poly-L-proline in Solution , 1960 .
[46] H. Bächinger. The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. , 1987, The Journal of biological chemistry.
[47] U. Hahn,et al. Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions. , 1990, Biochemistry.
[48] P. S. Kim,et al. Measurement of the β-sheet-forming propensities of amino acids , 1994, Nature.
[49] W. C. Johnson. Circular dichroism and its empirical application to biopolymers. , 1985, Methods of biochemical analysis.
[50] P E Wright,et al. Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins. , 1994, Methods in enzymology.
[51] H. Scheraga,et al. Chain-Folding Initiation Structures in Ribonuclease A: Conformational Analysis of trans-Ac-Asn-Pro-Tyr-NHMe (I) und trans-Ac-Tyr-Pro-Asn-NHMe (II) in Water und in the Solid State. , 1985 .
[52] H. Kessler,et al. Peptidkonformationen, II: 1H-NMR-Untersuchungen zur Konformation von cyclo(-Phe3Gly2-) , 1978 .
[53] Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. , 1991 .
[54] J E Wampler,et al. Occurrence and role of cis peptide bonds in protein structures. , 1990, Journal of molecular biology.
[55] A. Fersht,et al. Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding. , 1991, Biochemistry.
[56] J. Brandts,et al. Kinetic mechanism for conformational transitions between poly-L-prolines I and II: a study utilizing the cis-trans specificity of a proline-specific protease. , 1980, Biochemistry.
[57] G. Fischer,et al. FKBP‐like catalysis of peptidyl‐prolyl bond isomerization by micelles and membranes , 1997 .
[58] M. Williamson,et al. The structure and function of proline-rich regions in proteins. , 1994, The Biochemical journal.
[59] R Elber,et al. Kinetics of peptide folding: computer simulations of SYPFDV and peptide variants in water. , 1997, Journal of molecular biology.