Hinge-motion binding proteins: Unraveling their analytical potential

Elizabeth A. Moschou; Leonidas G. Bachas; Sylvia Daunert; Sapna K. Deo

doi:10.1021/ac069464r

Hinge-motion binding proteins: Unraveling their analytical potential

Elizabeth A. Moschou, Leonidas G. Bachas, Sylvia Daunert, Sapna K. Deo

Research output: Contribution to journal › Review article › peer-review

17 Scopus citations

Abstract

Among molecular recognition systems, hinge-motion binding proteins (HMBPs) demonstrate exquisite selectivity toward their corresponding ligand or analyte, with affinities down to the nanomolar range. Elizabeth A. Moschou, Leonidas G. Bachas, and Sylvia Daunert at the University of Kentucky and Sapna K. Deo at Indiana University-Purdue University Indianapolis focus on calmodulin and one class of HMBPs, the periplasmic binding proteins.

Original language	English (US)
Pages (from-to)	6692-6700
Number of pages	9
Journal	Analytical Chemistry
Volume	78
Issue number	19
DOIs	https://doi.org/10.1021/ac069464r
State	Published - Oct 1 2006
Externally published	Yes

ASJC Scopus subject areas

Analytical Chemistry

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10.1021/ac069464r

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abstract = "Among molecular recognition systems, hinge-motion binding proteins (HMBPs) demonstrate exquisite selectivity toward their corresponding ligand or analyte, with affinities down to the nanomolar range. Elizabeth A. Moschou, Leonidas G. Bachas, and Sylvia Daunert at the University of Kentucky and Sapna K. Deo at Indiana University-Purdue University Indianapolis focus on calmodulin and one class of HMBPs, the periplasmic binding proteins.",

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AU - Bachas, Leonidas G.

AU - Daunert, Sylvia

AU - Deo, Sapna K.

PY - 2006/10/1

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N2 - Among molecular recognition systems, hinge-motion binding proteins (HMBPs) demonstrate exquisite selectivity toward their corresponding ligand or analyte, with affinities down to the nanomolar range. Elizabeth A. Moschou, Leonidas G. Bachas, and Sylvia Daunert at the University of Kentucky and Sapna K. Deo at Indiana University-Purdue University Indianapolis focus on calmodulin and one class of HMBPs, the periplasmic binding proteins.

AB - Among molecular recognition systems, hinge-motion binding proteins (HMBPs) demonstrate exquisite selectivity toward their corresponding ligand or analyte, with affinities down to the nanomolar range. Elizabeth A. Moschou, Leonidas G. Bachas, and Sylvia Daunert at the University of Kentucky and Sapna K. Deo at Indiana University-Purdue University Indianapolis focus on calmodulin and one class of HMBPs, the periplasmic binding proteins.

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Hinge-motion binding proteins: Unraveling their analytical potential

Abstract

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