Structural analysis of peptides encompassing all α-helices of three α/β parallel proteins: Che-Y, flavodoxin and P21-Ras: Implications for α-Helix stability and the folding of α/β parallel proteins

[1]  S. Dasgupta,et al.  Design of helix ends. Amino acid preferences, hydrogen bonding and electrostatic interactions. , 2009, International journal of peptide and protein research.

[2]  M. Pincus,et al.  Comparisons between the three-dimensional structures of the chemotactic protein CheY and the normal Gly 12-p21 protein. , 2009, International journal of peptide and protein research.

[3]  V. Muñoz,et al.  Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. , 1995, Journal of molecular biology.

[4]  L Serrano,et al.  Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence. , 1995, Journal of molecular biology.

[5]  L Serrano,et al.  Helix stop and start signals in peptides and proteins. The capping box does not necessarily prevent helix elongation. , 1994, Journal of molecular biology.

[6]  R. L. Baldwin,et al.  Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i, i + 4. , 1994, Journal of molecular biology.

[7]  L. Serrano,et al.  A short linear peptide that folds into a native stable β-hairpin in aqueous solution , 1994, Nature Structural Biology.

[8]  Luis Serrano,et al.  Elucidating the folding problem of helical peptides using empirical parameters , 1994, Nature Structural Biology.

[9]  F. Blanco,et al.  NMR solution structure of the isolated N-terminal fragment of protein-G B1 domain. Evidence of trifluoroethanol induced native-like beta-hairpin formation. , 1994, Biochemistry.

[10]  L. Serrano,et al.  Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. , 1994, Journal of Molecular Biology.

[11]  T. Creighton,et al.  Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding. , 1993, Journal of molecular biology.

[12]  R. L. Baldwin,et al.  Effect of a single aspartate on helix stability at different positions in a neutral alanine‐based peptide , 1993, Protein science : a publication of the Protein Society.

[13]  R. L. Baldwin,et al.  The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide. , 1993, Biochemistry.

[14]  G. Rose,et al.  Helix stop signals in proteins and peptides: the capping box. , 1993, Biochemistry.

[15]  L. Serrano,et al.  1H- and 15N-NMR assignment and solution structure of the chemotactic Escherichia coli Che Y protein. , 1993, European journal of biochemistry.

[16]  H. Dyson,et al.  Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal. , 1993, Biochemistry.

[17]  R. L. Baldwin,et al.  Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. , 1993, Biochemistry.

[18]  J. Rizo,et al.  Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments. , 1993, Biochemistry.

[19]  C. Sander,et al.  How does the switch II region of G‐domains work? , 1993, FEBS letters.

[20]  R. L. Baldwin.  Pulsed H/D-exchange studies of folding intermediates , 1993 .

[21]  F. Blanco,et al.  CD and 1H-NMR studies on the conformational properties of peptide fragments from the C-terminal domain of thermolysin. , 1993, European journal of biochemistry.

[22]  P. Matsumura,et al.  Crystal structure of Escherichia coli CheY refined at 1.7-A resolution. , 1993, The Journal of biological chemistry.

[23]  R. L. Baldwin,et al.  Helical peptides with three pairs of Asp‐Arg and Glu‐Arg residues in different orientations and spacings , 1993, Protein science : a publication of the Protein Society.

[24]  D. Wemmer,et al.  Helix propagation in trifluoroethanol solutions , 1992, Biopolymers.

[25]  J. Neira,et al.  Peptide group chemical shift computation , 1992 .

[26]  R. Hodges,et al.  Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. , 1992, Biochemistry.

[27]  L Serrano,et al.  Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. , 1992, Journal of molecular biology.

[28]  P E Wright,et al.  Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. , 1992, Journal of molecular biology.

[29]  F. Blanco,et al.  Periodic properties of proton conformational shifts in isolated protein helices. An experimental study. , 1992, European journal of biochemistry.

[30]  A. Fersht,et al.  An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate. , 1992, Journal of molecular biology.

[31]  L Serrano,et al.  The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models. , 1992, Journal of molecular biology.

[32]  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.

[33]  F. Blanco,et al.  The homologous angiogenin and ribonuclease N-terminal fragments fold into very similar helices when isolated. , 1992, Biochemical and biophysical research communications.

[34]  F. Richards,et al.  Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. , 1991, Journal of molecular biology.

[35]  K Wüthrich,et al.  Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints , 1991, Journal of biomolecular NMR.

[36]  A Valencia,et al.  The ras protein family: evolutionary tree and role of conserved amino acids. , 1991, Biochemistry.

[37]  Y. Kawata,et al.  Use of fluorescence energy transfer to characterize the compactness of the constant fragment of an immunoglobulin light chain in the early stage of folding. , 1991, Biochemistry.

[38]  Y. Noda,et al.  Local structures in unfolded lysozyme and correlation with secondary structures in the native conformation: Helix‐forming or ‐breaking propensity of peptide segments , 1991, Biopolymers.

[39]  E. Stellwagen,et al.  Effect of amino acid ion pairs on peptide helicity. , 1991, Biochemistry.

[40]  L. Gierasch,et al.  Side chain–backbone hydrogen bonding contributes to helix stability in peptides derived from an α‐helical region of carboxypeptidase A , 1991, Proteins.

[41]  M. Williamson,et al.  Secondary‐structure dependent chemical shifts in proteins , 1990, Biopolymers.

[42]  W. Kabsch,et al.  Refined crystal structure of the triphosphate conformation of H‐ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. , 1990, The EMBO journal.

[43]  M. Sippl.  Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins. , 1990, Journal of molecular biology.

[44]  J. Tuls,et al.  Peptide alpha-helicity in aqueous trifluoroethanol: correlations with predicted alpha-helicity and the secondary structure of the corresponding regions of bovine growth hormone. , 1990, Biochemistry.

[45]  Alan R. Fersht,et al.  Capping and α-helix stability , 1989, Nature.

[46]  R. Woody,et al.  Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor. , 1989, Biochemistry.

[47]  R. L. Baldwin,et al.  Unusually stable helix formation in short alanine-based peptides. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[48]  N. Kallenbach,et al.  Persistence of the alpha-helix stop signal in the S-peptide in trifluoroethanol solutions. , 1989, Biochemistry.

[49]  M. Jiménez,et al.  Conformational properties of the isolated 1–23 fragment of human hemoglobin α-chain , 1988 .

[50]  J. Richardson,et al.  Amino acid preferences for specific locations at the ends of alpha helices. , 1988, Science.

[51]  G. Rose,et al.  Helix signals in proteins. , 1988, Science.

[52]  K. Wüthrich.  NMR of proteins and nucleic acids , 1988 .

[53]  Ad Bax,et al.  MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy , 1985 .

[54]  K Wüthrich,et al.  Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. , 1984, Journal of molecular biology.

[55]  W. Kabsch,et al.  Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.

[56]  F. Bermejo,et al.  Low‐temperature 1H‐NMR evidence of the folding of isolated ribonuclease S‐peptide , 1983, FEBS letters.

[57]  K. Wüthrich,et al.  Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. , 1983, Biochemical and biophysical research communications.

[58]  P. S. Kim,et al.  A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[59]  K Wüthrich,et al.  A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. , 1980, Biochemical and biophysical research communications.

[60]  M. Karplus,et al.  Protein-folding dynamics , 1976, Nature.

[61]  R. R. Ernst,et al.  Two‐dimensional spectroscopy. Application to nuclear magnetic resonance , 1976 .

[62]  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 .

[63]  Y H Chen,et al.  Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. , 1974, Biochemistry.

[64]  R. M. Burnett,et al.  The structure of the oxidized form of clostridial flavodoxin at 1.9-A resolution. , 1974, The Journal of biological chemistry.

[65]  A. Shrake,et al.  Environment and exposure to solvent of protein atoms. Lysozyme and insulin. , 1973, Journal of molecular biology.

[66]  L. Serrano.  Protein engineering and the dissection of protein folding pathways , 1994 .

[67]  J. Stock,et al.  Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks. , 1991, Annual review of biophysics and biophysical chemistry.

[68]  P E Wright,et al.  Defining solution conformations of small linear peptides. , 1991, Annual review of biophysics and biophysical chemistry.

[69]  N. D. Clarke,et al.  Identification of protein folds: Matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures , 1990, Proteins.

[70]  P. S. Kim,et al.  A helix stop signal in the isolated S-peptide of ribonuclease A , 1984, Nature.

[71]  G. Fasman,et al.  Circular dichroism and optical rotatory dispersion of proteins and polypeptides. , 1973, Methods in enzymology.