PMID: 9008361Dec 1, 1996Paper

Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling

Journal of Biomolecular NMR
I SethsonB H Jonsson

Abstract

The backbone NMR resonances of human carbonic anhydrase I (HCA I) have been assigned. This protein is one of the largest monomeric proteins assigned so far. The assignment was enabled by a combination of 3D triple-resonance experiments and extensive use of amino acid-specific 15N-labeling. The obtained resonance assignment has been used to evaluate the secondary structure elements present in solution. The solution structure appears to be very similar to the crystal structure, although some differences can be observed. Proton-deuteron exchange experiments have shown that the assignments provide probes that can be used in future studies of HCA I.

Citations

May 24, 2012·Biomolecular NMR Assignments·Shufen CaoMatthias Buck
Jan 9, 2015·PLoS Computational Biology·Markus NiklassonPatrik Lundström
Oct 1, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Celia Cabaleiro-Lago, Martin Lundqvist
May 26, 2021·The Journal of Physical Chemistry. B·Gediminas SkvarnavičiusVytautas Petrauskas
Dec 13, 2017·Analytical Chemistry·Daniel RozbeskýPetr Novák
Jun 15, 2005·Langmuir : the ACS Journal of Surfaces and Colloids·Martin LundqvistBengt-Harald Jonsson
Nov 17, 2004·Langmuir : the ACS Journal of Surfaces and Colloids·Martin LundqvistBengt-Harald Jonsson

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