High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy
暂无分享,去创建一个
[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.