High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR).

High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR). Research Abstract Details 

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High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR). Abstract Text:

Sunitha B Thakur,Qiuhong He,

Multidimensional electrophoretic NMR (nD-ENMR) is a potentially powerful tool for structural characterization of co-existing proteins and protein conformations. By applying a DC electric field pulse, the electrophoretic migration rates of different proteins were detected experimentally in a new dimension of electrophoretic flow. The electrophoretic mobilities were employed to differentiate protein signals. In U-shaped ENMR sample chambers, individual protein components in a solution mixture followed a cosinusoidal electrophoretic interferogram as a function of its unique electrophoretic migration rate. After Fourier transformation in the electrophoretic flow dimension, the protein signals were resolved at different resonant frequencies proportional to their electrophoretic mobilities. Currently, the mobility resolution of the proteins in the electrophoretic flow dimension is limited by severe truncations of the electrophoretic interferograms due to the finite electric field strength available before the onset of heat-induced convection. In this article, we present a successful signal processing method, the Burg's maximum entropy method (MEM), to analyze the truncated ENMR signals (MEM-ENMR). Significant enhancement in flow resolution was demonstrated using two-dimensional ENMR of two protein samples: a lysozyme solution and a solution mixture of bovine serum albumin (BSA) and ubiquitin. The electrophoretic mobilities of lysozyme, BSA and ubiquitin were measured from the MEM analysis as 7.5x10(-5), 1.9x10(-4) and 8.7x10(-5) cm2 V-1 s-1, respectively. Results from computer simulations confirmed a complete removal of truncation artifacts in the MEM-ENMR spectra with 3- to 6-fold resolution enhancement.

High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR). Publishing Authors By Initials

SB Thakur,Q He,

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High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR). Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of magnetic resonance (San Diego, Calif. :

VOLUME: 183

Page Numbers: 32-40

Journal Abbreviation: J. Magn. Reson.

ISSN: 1090-7807

DAY: 9

MONTH: 08

YEAR: 2006

High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR). Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9707935

High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR). Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: radiation effects

Chemical & Substance for Abstract: High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR). Information

Substance Name: Proteins

Registry Number: 0

Grant and Affiliation Information for High flow-resolution for mobility estimation in 2D-ENMR of proteins using maximum entropy method (MEM-ENMR).

AFFILIATION: Department of Medical Physics, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.

Country: United States

AGENCY: United States NCRR

GRANT: RR12774-01

ACRONYM: RR

MEDLINETA: J Magn Reson

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