Effect of isomerization of amino acid residues on the structure of aquaporin
β Scribed by A. V. Dmitriev; P. P. Isaev; V. A. Tverdislov
- Publisher
- SP MAIK Nauka/Interperiodica
- Year
- 2006
- Tongue
- English
- Weight
- 95 KB
- Volume
- 47
- Category
- Article
- ISSN
- 0022-4766
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The relative importance of three different routes for the N-nitrosation of amino acids (nitrosation by N 2 O 3 , by and by intramolecular migration of the nitroso group from the initially nitrosated carboxylate group) was investigated for methylaminobutyric acid, methylaminoisobutyric acid, azetidin
The aspartate residue (Asp 32) located in the complementarity-determining region (CDR) of a recombinant humanized monoclonal antibody (MAb I) is highly susceptible to the isomerization reaction. The modification of Asp 32 residue due to the isomerization reaction results in a significant reduction i
## Abstract ^13^C NMR spectroscopy is an excellent tool for studying the influence of __N__βprotecting groups on the __cis/trans__ isomerism of proline residues in proline peptides. This communication demonstrates the usefulness of ^13^C NMR spectroscopy in investigating conformational problems in