Refined solution structure of type III antifreeze protein: hydrophobic groups may be involved in the energetics of the protein-ice interaction.
暂无分享,去创建一个
[1] B. Sykes,et al. Effect of type III antifreeze protein dilution and mutation on the growth inhibition of ice. , 1996, Biophysical journal.
[2] S. Grzesiek,et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.
[3] L. Kay. Field gradient techniques in NMR spectroscopy. , 1995, Current opinion in structural biology.
[4] B. Sykes,et al. Solution secondary structure of calcium‐saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy , 1995, Protein science : a publication of the Protein Society.
[5] F. Sicheri,et al. Ice-binding structure and mechanism of an antifreeze protein from winter flounder , 1995, Nature.
[6] B. Sykes,et al. Comparative modeling of the three‐dimensional structure of Type II antifreeze protein , 1995, Protein science : a publication of the Protein Society.
[7] P. Davies,et al. Mixing antifreeze protein types changes ice crystal morphology without affecting antifreeze activity , 1995, FEBS letters.
[8] B. Sykes,et al. Quantification of the calcium‐induced secondary structural changes in the regulatory domain of troponin‐C , 1994, Protein science : a publication of the Protein Society.
[9] B. Sykes,et al. Structure‐function relationship in the globular type III antifreeze protein: Identification of a cluster of surface residues required for binding to ice , 1994, Protein science : a publication of the Protein Society.
[10] L. Kay,et al. Simultaneous Acquisition of 15N- and 13C-Edited NOE Spectra of Proteins Dissolved in H2O , 1994 .
[11] J. Engberts,et al. Hydrophobic Effects. Opinions and Facts , 1993 .
[12] B. Sykes,et al. Use of proline mutants to help solve the NMR solution structure of type III antifreeze protein , 1993, Protein science : a publication of the Protein Society.
[13] R. Laursen,et al. Structure-function relationships in an antifreeze polypeptide. The effect of added bulky groups on activity. , 1993, The Journal of biological chemistry.
[14] N. Colloc'h,et al. Comparison of three algorithms for the assignment of secondary structure in proteins: the advantages of a consensus assignment. , 1993, Protein engineering.
[15] L. Kay,et al. A Gradient-Enhanced HCCH-TOCSY Experiment for Recording Side-Chain 1H and 13C Correlations in H2O Samples of Proteins , 1993 .
[16] M. Goodgame,et al. HMQCJFIT - Software for Analyzing HMQC-J Spectra , 1993 .
[17] B D Sykes,et al. The nonhelical structure of antifreeze protein type III. , 1993, Science.
[18] G. Fletcher,et al. Herring antifreeze protein: primary structure and evidence for a C-type lectin evolutionary origin. , 1993, Molecular marine biology and biotechnology.
[19] Timothy F. Havel,et al. The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X‐ray structures , 1992, Protein science : a publication of the Protein Society.
[20] B. Rubinsky,et al. Structural and functional similarity between fish antifreeze proteins and calcium-dependent lectins. , 1992, Biochemical and biophysical research communications.
[21] J. Thornton,et al. Stereochemical quality of protein structure coordinates , 1992, Proteins.
[22] K. Sharp,et al. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons , 1991, Proteins.
[23] Robert Powers,et al. A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams , 1991 .
[24] C. Knight,et al. Adsorption of alpha-helical antifreeze peptides on specific ice crystal surface planes. , 1991, Biophysical journal.
[25] C. Hew,et al. Biochemistry of fish antifreeze proteins , 1990, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[26] Ad Bax,et al. Three-dimensional heteronuclear NMR of nitrogen-15 labeled proteins , 1989 .
[27] S. Fesik,et al. Heteronuclear three-dimensional nmr spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra , 1988 .
[28] A. Chakrabartty,et al. Crystal structure of an antifreeze polypeptide and its mechanistic implications , 1988, Nature.
[29] A. Gronenborn,et al. Determination of three‐dimensional structures of proteins from interproton distance data by hybrid distance geometry‐dynamical simulated annealing calculations , 1988, FEBS letters.
[30] H. Morris,et al. Primary and secondary structure of antifreeze peptides from arctic and antarctic zoarcid fishes. , 1987, Biochimica et biophysica acta.
[31] A M Lesk,et al. Interior and surface of monomeric proteins. , 1987, Journal of molecular biology.
[32] Mike Carson,et al. Ribbon models of macromolecules , 1987 .
[33] C. Hew,et al. Structure of an antifreeze polypeptide precursor from the sea raven, Hemitripterus americanus. , 1986, The Journal of biological chemistry.
[34] V. Ananthanarayanan,et al. Antifreeze proteins from the ocean pout, Macrozoarces americanus: circular dichroism spectral studies on the native and denatured states , 1986 .
[35] A. D. McLachlan,et al. Solvation energy in protein folding and binding , 1986, Nature.
[36] C. Hew,et al. Structure of an antifreeze polypeptide and its precursor from the ocean pout, Macrozoarces americanus. , 1985, The Journal of biological chemistry.
[37] D. G. Davis,et al. Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy , 1985 .
[38] T. Richmond,et al. Solvent accessible surface area and excluded volume in proteins. Analytical equations for overlapping spheres and implications for the hydrophobic effect. , 1984, Journal of molecular biology.
[39] A. L. Vries. Role of Glycopeptides and Peptides in Inhibition of Crystallization of Water in Polar Fishes , 1984 .
[40] K. Wüthrich,et al. Improved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filtering. , 1983, Biochemical and biophysical research communications.
[41] D. States,et al. A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants☆ , 1982 .
[42] Richard R. Ernst,et al. Investigation of exchange processes by two‐dimensional NMR spectroscopy , 1979 .
[43] J. Raymond,et al. Adsorption inhibition as a mechanism of freezing resistance in polar fishes. , 1977, Proceedings of the National Academy of Sciences of the United States of America.
[44] A. Shrake,et al. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. , 1973, Journal of molecular biology.
[45] Henry S. Frank,et al. Free Volume and Entropy in Condensed Systems III. Entropy in Binary Liquid Mixtures; Partial Molal Entropy in Dilute Solutions; Structure and Thermodynamics in Aqueous Electrolytes , 1945 .
[46] E. Driggers,et al. Adsorption to ice of fish antifreeze glycopeptides 7 and 8. , 1993, Biophysical journal.
[47] C. Hew,et al. Protein interaction with ice. , 1992, European journal of biochemistry.
[48] Axel T. Brunger,et al. X-PLOR Version 3.1: A System for X-ray Crystallography and NMR , 1992 .
[49] A. Devries,et al. The Role of Antifreeze Glycopeptides and Peptides in the Freezing Avoidance of Cold-Water Fish , 1991 .
[50] G. Prisco. Life Under Extreme Conditions , 1991, Springer Berlin Heidelberg.
[51] L. Kay,et al. New methods for the measurement of NHCαH coupling constants in 15N-labeled proteins , 1990 .
[52] Y. Yeh,et al. Antifreeze proteins from fish bloods. , 1978, Advances in protein chemistry.
[53] W. Kauzmann. Some factors in the interpretation of protein denaturation. , 1959, Advances in protein chemistry.
[54] L. Kay,et al. Three-Dimensional Heteronuclear NMR of 15 N-Labeled Proteins , 2022 .