Folding type‐specific secondary structure propensities of amino acids, derived from α‐helical, β‐sheet, α/β, and α+β proteins of known structures
暂无分享,去创建一个
Zhirong Sun | BoZhi Jiang | Bo Jiang | Tao Guo | Lei-Wei Peng | Zhi-Rong Sun | T. Guo | L. Peng
[1] Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. , 1993, Journal of molecular biology.
[2] W. DeGrado,et al. Protein Design: A Hierarchic Approach , 1995, Science.
[3] Yawen Bai,et al. Hydrogen bond strength and β‐sheet propensities: The role of a side chain blocking effect , 1994, Proteins.
[4] L. Regan,et al. Characterization of a helical protein designed from first principles. , 1988, Science.
[5] J. Richardson,et al. The anatomy and taxonomy of protein structure. , 1981, Advances in protein chemistry.
[6] Steven M. Muskal,et al. Predicting protein secondary structure content. A tandem neural network approach. , 1992, Journal of molecular biology.
[7] Robert L. Baldwin,et al. Relative helix-forming tendencies of nonpolar amino acids , 1990, Nature.
[8] A. Fersht. Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[9] A. Wallqvist,et al. A simplified amino acid potential for use in structure predictions of proteins , 1994, Proteins.
[10] P. S. Kim,et al. Measurement of the β-sheet-forming propensities of amino acids , 1994, Nature.
[11] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[12] A. Fersht,et al. Alpha-helix stability in proteins. II. Factors that influence stability at an internal position. , 1992, Journal of molecular biology.
[13] H. Scheraga,et al. Helix‐coil stability constants for the naturally occurring amino acids in water. XXIV. Half‐cystine parameters from random poly(hydroxybutylglutamine‐CO‐S‐methylthio‐L‐cysteine) , 1990 .
[14] C. Orengo,et al. Alpha plus beta folds revisited: some favoured motifs. , 1993, Structure.
[15] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[16] G J Barton,et al. Protein secondary structure prediction. , 1995, Current opinion in structural biology.
[17] G. Petsko,et al. Composition analysis of α-helices in thermophilic organisms , 1995 .
[18] K. Chou. A novel approach to predicting protein structural classes in a (20–1)‐D amino acid composition space , 1995, Proteins.
[19] N R Kallenbach,et al. Side chain contributions to the stability of alpha-helical structure in peptides. , 1990, Science.
[20] P. S. Kim,et al. Intermediates in the folding reactions of small proteins. , 1990, Annual review of biochemistry.
[21] P. Argos,et al. Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence. , 1996, Protein engineering.
[22] C. Chothia,et al. Structural patterns in globular proteins , 1976, Nature.
[23] G. Rose,et al. α‐Helix‐forming propensities in peptides and proteins , 1994 .
[24] L Regan,et al. A thermodynamic scale for the beta-sheet forming tendencies of the amino acids. , 1994, Biochemistry.
[25] J M Chandonia,et al. Neural networks for secondary structure and structural class predictions , 1995, Protein science : a publication of the Protein Society.
[26] W. DeGrado,et al. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. , 1990, Science.
[27] Jeremy M. Berg,et al. Thermodynamic β -sheet propensities measured using a zinc-finger host peptide , 1993, Nature.
[28] J. Thornton,et al. The influence of tertiary structure on secondary structure prediction , 1985 .
[29] B. Matthews,et al. Structural basis of amino acid alpha helix propensity. , 1993, Science.
[30] R. L. Baldwin,et al. Helix propensities of the amino acids measured in alanine‐based peptides without helix‐stabilizing side‐chain interactions , 1994, Protein science : a publication of the Protein Society.
[31] R. Srinivasan,et al. Local Interactions in Protein Folding: Lessons from the α-Helix* , 1997, The Journal of Biological Chemistry.