Improved Resolution from Double Constant-Time Evolution of 3D and 4D Triple-Resonance Experiments

The full text article is not available for purchase.

The publisher only permits individual articles to be downloaded by subscribers.


Triple-resonance NMR experiments are nearly essential for performing backbone assignments of proteins larger than ∼15 kDa. Our work extends the double constant-time (2CT) evolution scheme to triple-resonance 3D and 4D experiments. The modifications needed to accomplish 2CT evolution in triple resonance experiments are straight forward, are completely general, and consequently, will yield increased resolution for all out-and-back experiments. We expect that the increased resolution of experiments presented here will be useful in the study of larger proteins (>30 kDa) and in the study of highly helical proteins where1HN,15N, and13C dimensions are poorly dispersed.

Keywords: NMR; constant-time; triple-resonance

Document Type: Editorial

Affiliations: The Wistar Institute, 36th and Spruce Streets, Philadelphia, Pennsylvania, 19104

Publication date: February 1, 1998

Related content



Share Content

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
Cookie Policy
ingentaconnect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more