Agilent Ultra-fast NMR Spectroscopy in Cold Probes Application Note

This application note introduces a new method for studying the dynamics of biomolecules, based on ultrafast NMR spectroscopy and the performance of Varian cold probes.


Agilent Ultra-fast NMR Spectroscopy in Cold Probes Application Note - cover page
Brand
Agilent
Category
Other
Document type
Application Note
Language
English
Pages
2
File format
PDF
File size
961 KB
Published
12 June, 2012
Updated
30 September, 2023
Model
600MHz
MD5 checksum
3435E16827A56DB3666A0723E780FD6E

About this manual

This document describes the powerful combination of SOFAST NMR spectroscopy and Varian cold probe technology for studying the dynamics of bio-molecules, specifically proteins. It addresses the challenge of acquiring high-resolution data on large proteins quickly, which is difficult with standard 1-D or time-consuming 2-D NMR methods.

What's inside

  • Introduction
  • Experimental
  • Discussion
  • Conclusion
  • References

Specifications

Probe Type5mm Varian Triple Resonance Z-PFG cold probe
Recycle Time1 msec
Total Experimental Time (SOFAST)6 sec
Total Experimental Time (Standard HSQC)180 sec

Frequently asked questions

What is the key advantage of combining SOFAST with cold probes?

It allows the recording of 2-D NMR spectra of proteins in less than 10 sec, lowering the barrier to real-time investigation of dynamic events.

How long does the total experimental time take for the SOFAST-HMQC experiment on cytochrome C?

The total experimental time is 6 seconds.

What is the duty cycle increase when reducing the recycling delay in SOFAST experiments?

The duty cycle increases from the typical 8% to over 80%.

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