Works matching IS 02692139 AND DT 2000 AND VI 13 AND IP 8
Results: 11
Remarkable thermal stability of doubly intramolecularly cross-linked hen lysosyme.
- Published in:
- Protein Engineering, 2000, v. 13, n. 8, p. 602, doi. 10.1093/oxfordjournals.protein.a029827
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- Article
Characterization of function and activity of domains A, B and C of xylanase C from Fibrobacter succinogenes S85.
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- Protein Engineering, 2000, v. 13, n. 8, p. 593, doi. 10.1093/protein/13.8.593
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- Article
Phages from landscape libraries as substitute antibodies.
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- Protein Engineering, 2000, v. 13, n. 8, p. 589, doi. 10.1093/protein/13.8.589
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- Article
Construction of a diabody (small recombinant bispecific antibody) using a refolding system.
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- Protein Engineering, 2000, v. 13, n. 8, p. 583, doi. 10.1093/protein/13.8.583
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- Article
Characterization of diphtheria fusion proteins targeted to the human interleukin-3 receptor.
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- Protein Engineering, 2000, v. 13, n. 8, p. 575, doi. 10.1093/protein/13.8.575
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- Article
ScFv multimers of the anti-neuraminidase antibody NC10: shortening of the linker in single-chain Fv fragment assembled in VL to VH orientation drives the formation of dimers, trimers, tetramers and higher molecular mass multimers.
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- Protein Engineering, 2000, v. 13, n. 8, p. 565, doi. 10.1093/protein/13.8.565
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- Article
Replacement set mutagenesis of the four phosphate-binding arginine residues of thymidylate synthase.
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- Protein Engineering, 2000, v. 13, n. 8, p. 557, doi. 10.1093/protein/13.8.557
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- Article
Structural and interactional homology of clinically potential trypsin inhibitors: molecular modelling of Cucurbitaceae family peptides using the X-ray structure of MCTI-II.
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- Protein Engineering, 2000, v. 13, n. 8, p. 551, doi. 10.1093/protein/13.8.551
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- Article
Structure-derived substitution matrices for alignment of distantly related sequences.
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- Protein Engineering, 2000, v. 13, n. 8, p. 545, doi. 10.1093/protein/13.8.545
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- Article
Protein structure alignment using environmental profiles.
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- Protein Engineering, 2000, v. 13, n. 8, p. 535, doi. 10.1093/protein/13.8.535
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- Article
The initial step of the thermal unfolding of 3-isopropylmalate dehydrogenase detected by the temperature-jump Laue method.
- Published in:
- Protein Engineering, 2000, v. 13, n. 8, p. 527, doi. 10.1093/protein/13.8.527
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- Article