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The fibronectin type III domain as a scaffold for novel binding proteins.
Koide A, Bailey CW, Huang X, Koide S. Koide A, et al. Among authors: koide s. J Mol Biol. 1998 Dec 11;284(4):1141-51. doi: 10.1006/jmbi.1998.2238. J Mol Biol. 1998. PMID: 9837732
A dominant clone was expressed as a soluble protein and its properties were investigated in detail. Heteronuclear NMR characterization revealed that the selected mutant protein retains the global fold of FN3. It also has a modest conformational stability desp
A dominant clone was expressed as a soluble protein and its properties were investigated in detail. Heteronuclear NMR characte
Stabilization of a fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface.
Koide A, Jordan MR, Horner SR, Batori V, Koide S. Koide A, et al. Among authors: koide s. Biochemistry. 2001 Aug 28;40(34):10326-33. doi: 10.1021/bi010916y. Biochemistry. 2001. PMID: 11513611
Determination of pK(a)'s for all the side chain carboxyl groups of Asp and Glu residues revealed that Asp 23 and Glu 9 have an upshifted pK(a). ...These results indicate that repulsive interactions between like charges on the protein surface can destabilize a
Determination of pK(a)'s for all the side chain carboxyl groups of Asp and Glu residues revealed that Asp 23 and Glu 9 have an upshif …
Formation of the single-layer beta-sheet of Borrelia burgdorferi OspA in the absence of the C-terminal capping globular domain.
Huang X, Nakagawa T, Tamura A, Link K, Koide A, Koide S. Huang X, et al. Among authors: koide a, koide s. J Mol Biol. 2001 Apr 27;308(2):367-75. doi: 10.1006/jmbi.2001.4579. J Mol Biol. 2001. PMID: 11327773
Borrelia outer surface protein A (OspA) contains a unique single-layer beta-sheet that connects N and C-terminal globular domains. ...Thermal-denaturation experiments using differential scanning calorimetry and NMR spectroscopy revealed that the N-terminal globular …
Borrelia outer surface protein A (OspA) contains a unique single-layer beta-sheet that connects N and C-terminal globular doma …
Solution conformation and amyloid-like fibril formation of a polar peptide derived from a beta-hairpin in the OspA single-layer beta-sheet.
Ohnishi S, Koide A, Koide S. Ohnishi S, et al. Among authors: koide a, koide s. J Mol Biol. 2000 Aug 11;301(2):477-89. doi: 10.1006/jmbi.2000.3980. J Mol Biol. 2000. PMID: 10926522
A 23-residue peptide termed BH(9-10) was designed based on a beta-hairpin segment of the single-layer beta-sheet region of Borrelia OspA protein. ...In aqueous solution, the peptide was highly soluble and flexible, with a propensity to form a non-nativ
A 23-residue peptide termed BH(9-10) was designed based on a beta-hairpin segment of the single-layer beta-sheet region of Bor
Design of single-layer beta-sheets without a hydrophobic core.
Koide S, Huang X, Link K, Koide A, Bu Z, Engelman DM. Koide S, et al. Among authors: koide a. Nature. 2000 Jan 27;403(6768):456-60. doi: 10.1038/35000255. Nature. 2000. PMID: 10667801
Outer surface protein A (OspA) from Borrelia burgdorferi contains a three-stranded beta-sheet segment which connects two globular domains. Although this single-layer beta-sheet segment is exposed to solvent on both faces and thus does not contain a hydrophobi …
Outer surface protein A (OspA) from Borrelia burgdorferi contains a three-stranded beta-sheet segment which connects two globu …
A stable single-layer beta-sheet without a hydrophobic core.
Pham TN, Koide A, Koide S. Pham TN, et al. Among authors: koide a, koide s. Nat Struct Biol. 1998 Feb;5(2):115-9. doi: 10.1038/nsb0298-115. Nat Struct Biol. 1998. PMID: 9461076
Outer surface protein A from the Lyme disease spirochete Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. ...
Outer surface protein A from the Lyme disease spirochete Borrelia burgdorferi contains a single-layer beta-sheet connecting th …
The roles of turn formation and cross-strand interactions in fibrillization of peptides derived from the OspA single-layer beta-sheet.
Ohnishi S, Koide A, Koide S. Ohnishi S, et al. Among authors: koide a, koide s. Protein Sci. 2001 Oct;10(10):2083-92. doi: 10.1110/ps.15901. Protein Sci. 2001. PMID: 11567099 Free PMC article.
We previously demonstrated that a beta-hairpin peptide, termed BH(9-10), derived from a single-layer beta-sheet of Borrelia OspA protein, formed a native-like beta-turn in trifluoroethanol (TFE) solution, and it assembled into amyloid-like fibrils at higher T …
We previously demonstrated that a beta-hairpin peptide, termed BH(9-10), derived from a single-layer beta-sheet of Borrelia Os …
Crystal structure of Aspergillus niger isopullulanase, a member of glycoside hydrolase family 49.
Mizuno M, Koide A, Yamamura A, Akeboshi H, Yoshida H, Kamitori S, Sakano Y, Nishikawa A, Tonozuka T. Mizuno M, et al. Among authors: koide a. J Mol Biol. 2008 Feb 8;376(1):210-20. doi: 10.1016/j.jmb.2007.11.098. Epub 2007 Dec 5. J Mol Biol. 2008. PMID: 18155243
Domain N consists of 13 beta-strands and forms a beta-sandwich. Domain C, where the active site is located, forms a right-handed beta-helix, and the lengths of the pitches of each coil of the beta-helix are similar to those of GH49 dextranase and GH28 polygalacturon …
Domain N consists of 13 beta-strands and forms a beta-sandwich. Domain C, where the active site is located, forms a right-hand …
Crystallization and properties of carboxypeptidase A gamma from porcine pancreas.
Koide A, Yoshizawa M, Kurachi K. Koide A, et al. Eur J Biochem. 1981 Jul;117(2):383-8. doi: 10.1111/j.1432-1033.1981.tb06349.x. Eur J Biochem. 1981. PMID: 7274215
The apparent relative molecular mass determined by gel filtration on a Sephadex G-200 column was 38 900. The amino-terminal sequence of the porcine carboxypeptidase A gamma was Asn-Tyr-Ala-Thr-Tyr-His-Thr-Leu-Glu-Glu-Ile-Tyr-Asp-Phe-Met-Asp-Ile-Leu-Val-Ala -Glu-His- …
The apparent relative molecular mass determined by gel filtration on a Sephadex G-200 column was 38 900. The amino-terminal sequence …
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