Literature DB >> 19307141

H-start for exclusively heteronuclear NMR spectroscopy: the case of intrinsically disordered proteins.

Wolfgang Bermel1, Ivano Bertini, Veronika Csizmok, Isabella C Felli, Roberta Pierattelli, Peter Tompa.   

Abstract

Here, we present a series of exclusively heteronuclear multidimensional NMR experiments, based on 13C direct detection, which exploit the (1)H polarization as a starting source to increase the signal-to-noise ratio. This contributes to make this spectroscopy more useful and usable. Examples are reported for a suitable system such as securin, an intrinsically disordered protein of 22 kDa.

Entities:  

Mesh：

Substances：

Year:  2009        PMID： 19307141     DOI： 10.1016/j.jmr.2009.02.012

Source DB:  PubMed          Journal:  J Magn Reson        ISSN： 1090-7807            Impact factor:   2.229


  34 in total

1.  Speeding up sequence specific assignment of IDPs.

Authors:  Wolfgang Bermel; Ivano Bertini; Isabella C Felli; Leonardo Gonnelli; Wiktor Koźmiński; Alessandro Piai; Roberta Pierattelli; Jan Stanek
Journal:  J Biomol NMR       Date:  2012-06-10       Impact factor: 2.835

2.  HA-detected experiments for the backbone assignment of intrinsically disordered proteins.

Authors:  Sampo Mäntylahti; Olli Aitio; Maarit Hellman; Perttu Permi
Journal:  J Biomol NMR       Date:  2010-05-01       Impact factor: 2.835

3.  Direct ¹³C-detected NMR experiments for mapping and characterization of hydrogen bonds in RNA.

Authors:  Boris Fürtig; Robbin Schnieders; Christian Richter; Heidi Zetzsche; Sara Keyhani; Christina Helmling; Helena Kovacs; Harald Schwalbe
Journal:  J Biomol NMR       Date:  2016-02-06       Impact factor: 2.835

4.  4D non-uniformly sampled HCBCACON and ¹J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins.

Authors:  Jiří Nováček; Noam Y Haba; Jordan H Chill; Lukáš Zídek; Vladimír Sklenář
Journal:  J Biomol NMR       Date:  2012-05-13       Impact factor: 2.835

5.  Bridge over troubled proline: assignment of intrinsically disordered proteins using (HCA)CON(CAN)H and (HCA)N(CA)CO(N)H experiments concomitantly with HNCO and i(HCA)CO(CA)NH.

Authors:  Maarit Hellman; Henni Piirainen; Veli-Pekka Jaakola; Perttu Permi
Journal:  J Biomol NMR       Date:  2013-12-18       Impact factor: 2.835

6.  Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c.

Authors:  Jiří Nováček; Lubomír Janda; Radka Dopitová; Lukáš Žídek; Vladimír Sklenář
Journal:  J Biomol NMR       Date:  2013-07-23       Impact factor: 2.835

7.  Direct correlation of consecutive C'-N groups in proteins: a method for the assignment of intrinsically disordered proteins.

Authors:  David Pantoja-Uceda; Jorge Santoro
Journal:  J Biomol NMR       Date:  2013-08-09       Impact factor: 2.835

8.  High-dimensionality 13C direct-detected NMR experiments for the automatic assignment of intrinsically disordered proteins.

Authors:  Wolfgang Bermel; Isabella C Felli; Leonardo Gonnelli; Wiktor Koźmiński; Alessandro Piai; Roberta Pierattelli; Anna Zawadzka-Kazimierczuk
Journal:  J Biomol NMR       Date:  2013-11-08       Impact factor: 2.835

9.  NMR structure analysis of uniformly 13C-labeled carbohydrates.

Authors:  Carolina Fontana; Helena Kovacs; Göran Widmalm
Journal:  J Biomol NMR       Date:  2014-04-26       Impact factor: 2.835

Review 10.  In-Cell NMR Spectroscopy of Intrinsically Disordered Proteins.

Authors:  Nicholas Sciolino; David S Burz; Alexander Shekhtman
Journal:  Proteomics       Date:  2019-01-15       Impact factor: 3.984
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.