Direct detection of lysine side chain NH3+ in protein-heparin complexes using NMR spectroscopy

Krishna Mohan Sepuru; Junji Iwahara; Krishna Rajarathnam

doi:10.1039/c7an01406f

Direct detection of lysine side chain NH₃⁺ in protein-heparin complexes using NMR spectroscopy

Krishna Mohan Sepuru, Junji Iwahara, Krishna Rajarathnam

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

Two NMR observables, the N_ζH₃⁺ peak in the HISQC spectrum and N_ζ chemical shift difference between the free and heparin-bound forms, can identify binding-interface lysines in protein-heparin complexes. Unlike backbone chemical shifts, these direct probes are stringent and are less prone to either false positives or false negatives.

Original language	English (US)
Pages (from-to)	635-638
Number of pages	4
Journal	Analyst
Volume	143
Issue number	3
DOIs	https://doi.org/10.1039/c7an01406f
State	Published - Feb 7 2018

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry
Environmental Chemistry
Spectroscopy
Electrochemistry

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10.1039/c7an01406f

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abstract = "Two NMR observables, the NζH3+ peak in the HISQC spectrum and Nζ chemical shift difference between the free and heparin-bound forms, can identify binding-interface lysines in protein-heparin complexes. Unlike backbone chemical shifts, these direct probes are stringent and are less prone to either false positives or false negatives.",

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AB - Two NMR observables, the NζH3+ peak in the HISQC spectrum and Nζ chemical shift difference between the free and heparin-bound forms, can identify binding-interface lysines in protein-heparin complexes. Unlike backbone chemical shifts, these direct probes are stringent and are less prone to either false positives or false negatives.

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Direct detection of lysine side chain NH₃⁺ in protein-heparin complexes using NMR spectroscopy

Abstract

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