The Influence of Protecting Groups on the β-Sheet-Structure Stability of Protected Peptides^<1)>
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概要
- 論文の詳細を見る
- 1996-05-15
著者
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NARITA Mitsuaki
Department of Biotechnology, Tokyo University of Agriculture and Technology
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Narita M
Tokyo Univ. Agriculture And Technol. Tokyo
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Narita Mitsuaki
Department Of Biotechnology And Life Science Faculty Of Technology Tokyo University Of Agriculture A
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Narita Mitsuaki
Department Of Biotechnology Faculty Of Technology Tokyo University Of Agriculture And Technology
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Narita Mitsuaki
Department Of Biotechnology Faculty Of Technology University Of Agriculture And Technology
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OH-UCHI Sho-kichi
Department of Biotechnology, Faculty of Technology, Tokyo University of Agriculture and Technology
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LEE Jin-Shik
Department of Biotechnology, Faculty of Technology, Tokyo University of Agriculture and Technology
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Lee Jin-shik
Department Of Biotechnology Faculty Of Technology Tokyo University Of Agriculture And Technology
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Oh-uchi Sho-kichi
Department Of Biotechnology Faculty Of Technology Tokyo University Of Agriculture And Technology
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- A New Type of Φ, Ψ Representation of the Protein Tertiary Structure and the Analysis of the Amino Acid Preferences for Speciffic Locations at Type-II β-Turn by Using 8000 Possible Kinds of Amino Acid Residues
- Statistical Characterization of Eleven Kinds of Helix Elements with Amino Acid Residues in the Middle of Triplets
- Conformations of Synthetic Model Peptides for Plasmodium falciparum Circumsporozoite Protein in Me_2SO by ^1H NMR and Distance Geometry Calculations
- Only Weak Dependence of the Protected Peptides Solubility in Organic Solvents on Their Amino Acid Sequence
- The Influence of Protecting Groups on the β-Sheet-Structure Stability of Protected Peptides^
- Assingments of Tri- and Tetrapeptide Sequences in Globular Proteins to the 18 Kinds of Local Structures along Helices and Their Propensities for Specific Local Structures
- Syntheses and properties of oligo-L-leucines containing .ALPHA.-aminoisobutyric acid residues. The novel strategy for solubility improvement in helical oligopeptides based on the restriction of the values of the backbone dihedral angles .PHI. and .PSI. of
- The ability of an .ALPHA.-aminoisobutyric acid residue to promote helical folding in oligopeptides.
- Individuality of amino acid residues in protected peptides. Conformational and .BETA.-sheet structure-disrupted behaviors of resin-bound peptides.
- Conformations in the solid state and solubility properties of protected homooligopeptides of glycine and .BETA.-alanine.
- Liquid phase peptide synthesis by fragment condensation on soluble polymer support. IV. Relative reactivities of N-t-butoxycarbonyl(Boc)amino acids and Boc-oligopeptide acids in their esterification with soluble chloromethylated polystyrene.
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- Infrared absorption study of human hemoglobin .ALPHA.-chain (123-136) fragments in dichloromethane.
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- Design of the synthetic route for helical peptides. Synthesis and solubility of model peptides having a helical structure.
- The easy disruption of the .BETA.-sheet structure of resin-bound human proinsulin C-peptide fragments by strong electron-donor solvents.
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- The electron donor-acceptor interaction between mixed solvents and its influence on their .BETA.-sheet strucutre-disrupting potential.
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- The solubility of peptide intermediates in organic solvents. Solubilizing potential of hexafluoro-2-propanol.
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- The study on peptide and protein syntheses. Infrared spectroscopic conformational analysis of oligo-L-leucines containing only one D-amino acid residue.
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