Literature DB >> 26293126

Stable isotope labeling strategy based on coding theory.

Takuma Kasai1,2, Seizo Koshiba1,3, Jun Yokoyama1,4,5, Takanori Kigawa6,7,8,9.   

Abstract

We describe a strategy for stable isotope-aided protein nuclear magnetic resonance (NMR) analysis, called stable isotope encoding. The basic idea of this strategy is that amino-acid selective labeling can be considered as "encoding and decoding" processes, in which the information of amino acid type is encoded by the stable isotope labeling ratio of the corresponding residue and it is decoded by analyzing NMR spectra. According to the idea, the strategy can diminish the required number of labelled samples by increasing information content per sample, enabling discrimination of 19 kinds of non-proline amino acids with only three labeled samples. The idea also enables this strategy to combine with information technologies, such as error detection by check digit, to improve the robustness of analyses with low quality data. Stable isotope encoding will facilitate NMR analyses of proteins under non-ideal conditions, such as those in large complex systems, with low-solubility, and in living cells.

Entities:  

Keywords:  Amino-acid selective stable isotope labeling; Cell-free protein synthesis; Coding theory; Combinatorial selective labeling; Signal assignment

Mesh:

Year:  2015        PMID: 26293126     DOI: 10.1007/s10858-015-9978-8

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN: 0925-2738            Impact factor:   2.835


  27 in total

Review 1.  Amino acid selective labeling and unlabeling for protein resonance assignments.

Authors:  Garima Jaipuria; B Krishnarjuna; Somnath Mondal; Abhinav Dubey; Hanudatta S Atreya
Journal:  Adv Exp Med Biol       Date:  2012       Impact factor: 2.622

2.  Long-range effects and functional consequences of stabilizing mutations in the ankyrin repeat domain of IκBα.

Authors:  Carla F Cervantes; Lindsey D Handley; Shih-Che Sue; H Jane Dyson; Elizabeth A Komives
Journal:  J Mol Biol       Date:  2012-12-26       Impact factor: 5.469

3.  NMRPipe: a multidimensional spectral processing system based on UNIX pipes.

Authors:  F Delaglio; S Grzesiek; G W Vuister; G Zhu; J Pfeifer; A Bax
Journal:  J Biomol NMR       Date:  1995-11       Impact factor: 2.835

4.  Optimization of amino acid type-specific 13C and 15N labeling for the backbone assignment of membrane proteins by solution- and solid-state NMR with the UPLABEL algorithm.

Authors:  Frederik Hefke; Anurag Bagaria; Sina Reckel; Sandra Johanna Ullrich; Volker Dötsch; Clemens Glaubitz; Peter Güntert
Journal:  J Biomol NMR       Date:  2010-12-18       Impact factor: 2.835

5.  Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment.

Authors:  Frank Löhr; Sina Reckel; Mikhail Karbyshev; Peter J Connolly; Norzehan Abdul-Manan; Frank Bernhard; Jonathan M Moore; Volker Dötsch
Journal:  J Biomol NMR       Date:  2012-01-18       Impact factor: 2.835

6.  Improving cell-free protein synthesis for stable-isotope labeling.

Authors:  Takayoshi Matsuda; Seizo Koshiba; Naoya Tochio; Eiko Seki; Noriyuki Iwasaki; Takashi Yabuki; Makoto Inoue; Shigeyuki Yokoyama; Takanori Kigawa
Journal:  J Biomol NMR       Date:  2007-01-20       Impact factor: 2.835

7.  Protein signal assignments using specific labeling and cell-free synthesis.

Authors:  Jianxia Shi; Jeffrey G Pelton; Ho S Cho; David E Wemmer
Journal:  J Biomol NMR       Date:  2004-03       Impact factor: 2.835

8.  Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.

Authors:  Eric B Bertelsen; Lyra Chang; Jason E Gestwicki; Erik R P Zuiderweg
Journal:  Proc Natl Acad Sci U S A       Date:  2009-05-13       Impact factor: 11.205

9.  Cell-free protein synthesis system from Escherichia coli cells cultured at decreased temperatures improves productivity by decreasing DNA template degradation.

Authors:  Eiko Seki; Natsuko Matsuda; Shigeyuki Yokoyama; Takanori Kigawa
Journal:  Anal Biochem       Date:  2008-03-07       Impact factor: 3.365

10.  A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.

Authors:  M Ikura; L E Kay; A Bax
Journal:  Biochemistry       Date:  1990-05-15       Impact factor: 3.162

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  2 in total

1.  CombLabel: rational design of optimized sequence-specific combinatorial labeling schemes. Application to backbone assignment of membrane proteins with low stability.

Authors:  M Yu Myshkin; M A Dubinnyi; D S Kulbatskii; E N Lyukmanova; M P Kirpichnikov; Z O Shenkarev
Journal:  J Biomol NMR       Date:  2019-07-08       Impact factor: 2.835

2.  Amino-acid selective isotope labeling enables simultaneous overlapping signal decomposition and information extraction from NMR spectra.

Authors:  Takuma Kasai; Shunsuke Ono; Seizo Koshiba; Masayuki Yamamoto; Toshiyuki Tanaka; Shiro Ikeda; Takanori Kigawa
Journal:  J Biomol NMR       Date:  2020-01-30       Impact factor: 2.835

  2 in total

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