Kawata Y - Search Results

1

Chemical modification of tryptophan residues and stability changes in proteins.

Okajima T, Kawata Y, Hamaguchi K. Okajima T, et al. Among authors: kawata y. Biochemistry. 1990 Oct 2;29(39):9168-75. doi: 10.1021/bi00491a010. Biochemistry. 1990. PMID: 2125474

2

Hydrogen-exchange kinetics of the indole NH proton of the buried tryptophan in the constant fragment of the immunoglobulin light chain.

Kawata Y, Goto Y, Hamaguchi K, Hayashi F, Kobayashi Y, Kyogoku Y. Kawata Y, et al. Biochemistry. 1988 Jan 12;27(1):346-50. doi: 10.1021/bi00401a052. Biochemistry. 1988. PMID: 2831958

3

Unfolding and refolding of a type kappa immunoglobulin light chain and its variable and constant fragments.

Tsunenaga M, Goto Y, Kawata Y, Hamaguchi K. Tsunenaga M, et al. Among authors: kawata y. Biochemistry. 1987 Sep 22;26(19):6044-51. doi: 10.1021/bi00393a015. Biochemistry. 1987. PMID: 3120770

4

Stability of ribonuclease T2 from Aspergillus oryzae.

Kawata Y, Hamaguchi K. Kawata Y, et al. Protein Sci. 1995 Mar;4(3):416-20. doi: 10.1002/pro.5560040308. Protein Sci. 1995. PMID: 7795525 Free PMC article.

5

Use of fluorescence energy transfer to characterize the compactness of the constant fragment of an immunoglobulin light chain in the early stage of folding.

Kawata Y, Hamaguchi K. Kawata Y, et al. Biochemistry. 1991 May 7;30(18):4367-73. doi: 10.1021/bi00232a001. Biochemistry. 1991. PMID: 1902379

6

Conformation and disulfide bond formation of the constant fragment of an immunoglobulin light chain: effect of truncation at the C-terminal region.

Ishiwata A, Kawata Y, Hamaguchi K. Ishiwata A, et al. Among authors: kawata y. Biochemistry. 1991 Aug 6;30(31):7766-71. doi: 10.1021/bi00245a014. Biochemistry. 1991. PMID: 1907845

7

Conformations of isolated fragments of pancreatic polypeptide.

Tonan K, Kawata Y, Hamaguchi K. Tonan K, et al. Among authors: kawata y. Biochemistry. 1990 May 8;29(18):4424-9. doi: 10.1021/bi00470a023. Biochemistry. 1990. PMID: 2350546

8

Extrinsic 33-kilodalton protein of spinach oxygen-evolving complexes: kinetic studies of folding and disulfide reduction.

Tanaka S, Kawata Y, Wada K, Hamaguchi K. Tanaka S, et al. Among authors: kawata y. Biochemistry. 1989 Sep 5;28(18):7188-93. doi: 10.1021/bi00444a009. Biochemistry. 1989. PMID: 2684273

9

Conformation of the constant fragment of the immunoglobulin light chain: effect of cleavage of the polypeptide chain and the disulfide bond.

Goto Y, Tsunenaga M, Kawata Y, Hamaguchi K. Goto Y, et al. Among authors: kawata y. J Biochem. 1987 Feb;101(2):319-29. doi: 10.1093/oxfordjournals.jbchem.a121916. J Biochem. 1987. PMID: 3108243 Free article.

10

Global fluctuations of the immunoglobulin domains under physiological conditions.

Kawata Y, Hamaguchi K. Kawata Y, et al. Biopolymers. 1990;30(3-4):389-94. doi: 10.1002/bip.360300316. Biopolymers. 1990. PMID: 2126211

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