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Literature DB >> 1889645

Combined differential light scattering with various liquid chromatography separation techniques.

P J Wyatt¹.

Abstract

Mesh：

Year: 1991 PMID： 1889645 DOI： 10.1042/bst0190485

Source DB: PubMed Journal: Biochem Soc Trans ISSN： 0300-5127 Impact factor: 5.407

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8 in total

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2. A structural model for the damage-sensing complex in bacterial nucleotide excision repair.

Authors: Danaya Pakotiprapha; Yi Liu; Gregory L Verdine; David Jeruzalmi
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3. Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150.

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4. Retinal degeneration 3 (RD3) protein, a retinal guanylyl cyclase regulator, forms a monomeric and elongated four-helix bundle.

Authors: Igor V Peshenko; Qinhong Yu; Sunghyuk Lim; Diana Cudia; Alexander M Dizhoor; James B Ames
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5. NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection.

Authors: Xianzhong Xu; Wei Xu; Josep Rayo; Yuko Ishida; Walter S Leal; James B Ames
Journal: Biochemistry Date: 2010-02-23 Impact factor: 3.162

Combined differential light scattering with various liquid chromatography separation techniques.

1. Structural basis for Ca2+-induced activation and dimerization of estrogen receptor α by calmodulin.

2. A structural model for the damage-sensing complex in bacterial nucleotide excision repair.

3. Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150.

4. Retinal degeneration 3 (RD3) protein, a retinal guanylyl cyclase regulator, forms a monomeric and elongated four-helix bundle.

5. NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection.

6. NMR and EPR-DEER Structure of a Dimeric Guanylate Cyclase Activator Protein-5 from Zebrafish Photoreceptors.

7. Structural basis for sequence specific DNA binding and protein dimerization of HOXA13.

8. Effect of frozen storage on molecular weight, size distribution and conformation of gluten by SAXS and SEC-MALLS.