Applications of saturation transfer difference NMR in biological systems

The method of saturation transfer difference (STD) nuclear magnetic resonance (NMR) is an indispensable NMR tool in drug discovery. It identifies binding epitope(s) at the atomic resolution of small molecule ligands (e.g. organic drugs, peptides and oligosaccharides), while interacting with their re...

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Main Authors: Bhunia, Anirban, Bhattacharjya, Surajit, Chatterjee, Subhrangsu
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2013
Online Access:https://hdl.handle.net/10356/97921
http://hdl.handle.net/10220/13241
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-979212020-03-07T12:18:18Z Applications of saturation transfer difference NMR in biological systems Bhunia, Anirban Bhattacharjya, Surajit Chatterjee, Subhrangsu School of Biological Sciences The method of saturation transfer difference (STD) nuclear magnetic resonance (NMR) is an indispensable NMR tool in drug discovery. It identifies binding epitope(s) at the atomic resolution of small molecule ligands (e.g. organic drugs, peptides and oligosaccharides), while interacting with their receptors, such as proteins and/or nucleic acids. The method is widely used to screen active drug molecules, simultaneously ranking them in a qualitative way. STD NMR is highly successful for a variety of high molecular weight systems, such as whole viruses, platelets, intact cells, lipopolysaccharide micelles, membrane proteins, recombinant proteins and dispersion pigments. Modifications of STD pulse programs using 13C and 15N nuclei are now used to overcome the signal overlapping that occurs with more complex structures. 2013-08-27T06:02:34Z 2019-12-06T19:48:22Z 2013-08-27T06:02:34Z 2019-12-06T19:48:22Z 2012 2012 Journal Article Bhunia, A., Bhattacharjya, S., & Chatterjee, S. (2012). Applications of saturation transfer difference NMR in biological systems. Drug Discovery Today, 17(9-10), 505-513. https://hdl.handle.net/10356/97921 http://hdl.handle.net/10220/13241 10.1016/j.drudis.2011.12.016 en Drug discovery today
institution Nanyang Technological University
building NTU Library
country Singapore
collection DR-NTU
language English
description The method of saturation transfer difference (STD) nuclear magnetic resonance (NMR) is an indispensable NMR tool in drug discovery. It identifies binding epitope(s) at the atomic resolution of small molecule ligands (e.g. organic drugs, peptides and oligosaccharides), while interacting with their receptors, such as proteins and/or nucleic acids. The method is widely used to screen active drug molecules, simultaneously ranking them in a qualitative way. STD NMR is highly successful for a variety of high molecular weight systems, such as whole viruses, platelets, intact cells, lipopolysaccharide micelles, membrane proteins, recombinant proteins and dispersion pigments. Modifications of STD pulse programs using 13C and 15N nuclei are now used to overcome the signal overlapping that occurs with more complex structures.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Bhunia, Anirban
Bhattacharjya, Surajit
Chatterjee, Subhrangsu
format Article
author Bhunia, Anirban
Bhattacharjya, Surajit
Chatterjee, Subhrangsu
spellingShingle Bhunia, Anirban
Bhattacharjya, Surajit
Chatterjee, Subhrangsu
Applications of saturation transfer difference NMR in biological systems
author_sort Bhunia, Anirban
title Applications of saturation transfer difference NMR in biological systems
title_short Applications of saturation transfer difference NMR in biological systems
title_full Applications of saturation transfer difference NMR in biological systems
title_fullStr Applications of saturation transfer difference NMR in biological systems
title_full_unstemmed Applications of saturation transfer difference NMR in biological systems
title_sort applications of saturation transfer difference nmr in biological systems
publishDate 2013
url https://hdl.handle.net/10356/97921
http://hdl.handle.net/10220/13241
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