High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy

[1]  K. Kuwajima Stopped-Flow Circular Dichroism , 1996 .

[2]  T. Tanaka,et al.  High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein. , 1995, Journal of molecular biology.

[3]  Dudley H. Williams,et al.  A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin , 1995, Nature Structural Biology.

[4]  C. Dobson,et al.  Conformational properties of four peptides spanning the sequence of hen lysozyme. , 1995, Journal of molecular biology.

[5]  A. Wada,et al.  Stability of α-helices in a molten globule state of cytochrome c by hydrogen-deuterium exchange and two-dimensional NMR spectroscopy , 1995 .

[6]  R. L. Baldwin The nature of protein folding pathways: The classical versus the new view , 1995, Journal of biomolecular NMR.

[7]  K. Nishikawa,et al.  Trifluoroethanol-induced Stabilization of the α-Helical Structure of β-Lactoglobulin: Implication for Non-hierarchical Protein Folding , 1995 .

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

[9]  S. Radford,et al.  Far-UV circular dichroism reveals a conformational switch in a peptide fragment from the beta-sheet of hen lysozyme. , 1994, Biochemistry.

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

[11]  B. Rost,et al.  Combining evolutionary information and neural networks to predict protein secondary structure , 1994, Proteins.

[12]  Burkhard Rost,et al.  PHD - an automatic mail server for protein secondary structure prediction , 1994, Comput. Appl. Biosci..

[13]  P E Wright,et al.  Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. , 1993, Science.

[14]  H. Roder,et al.  A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. , 1993, Biochemistry.

[15]  B. Rost,et al.  Prediction of protein secondary structure at better than 70% accuracy. , 1993, Journal of molecular biology.

[16]  P E Wright,et al.  Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. , 1993, Biochemistry.

[17]  E. Dufour,et al.  Reversible effects of medium dielectric constant on structural transformation of β‐lactoglobulin and its retinol binding , 1993, Biopolymers.

[18]  Y. Kuroda,et al.  Residual helical structure in the C-terminal fragment of cytochrome c. , 1993, Biochemistry.

[19]  H. Dyson,et al.  Peptide conformation and protein folding , 1993 .

[20]  D. Craik,et al.  A peptide corresponding to the N‐terminal 13 residues of T4 lysozyme forms an α‐helix , 1993 .

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

[22]  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.

[23]  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.

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

[25]  R. L. Baldwin,et al.  Parameters of helix–coil transition theory for alanine‐based peptides of varying chain lengths in water , 1991, Biopolymers.

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

[27]  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.

[28]  K Nishikawa,et al.  Predicting protein secondary structure based on amino acid sequence. , 1991, Methods in enzymology.

[29]  S W Englander,et al.  Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR. , 1990, Biochemistry.

[30]  P E Wright,et al.  Structural characterization of a partly folded apomyoglobin intermediate. , 1990, Science.

[31]  J. Collawn,et al.  Stabilization of helical structure in two 17‐residue amphipathic analogues of the C‐terminal peptide of cytochrome c , 1990, Biopolymers.

[32]  Terrence G. Oas,et al.  A peptide model of a protein folding intermediate , 1988, Nature.

[33]  S. Walter Englander,et al.  Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR , 1988, Nature.

[34]  P E Wright,et al.  Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. , 1988, Biochemistry.

[35]  S Sugai,et al.  Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism , 1987, FEBS letters.

[36]  Robert L. Baldwin,et al.  Tests of the helix dipole model for stabilization of α-helices , 1987, Nature.

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

[38]  P. Kraulis,et al.  The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein , 1986, Nature.

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

[40]  N. Go Theoretical studies of protein folding. , 1983, Annual review of biophysics and bioengineering.

[41]  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.

[42]  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.

[43]  Y H Chen,et al.  Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. , 1972, Biochemistry.

[44]  J. E. Brown,et al.  Helix-coil transition of the isolated amino terminus of ribonuclease. , 1971, Biochemistry.