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Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli

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title

Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli (English)

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1 reference

2

J I Gordon

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author name string

J C Sacchettini

series ordinal

1

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L J Banaszak

series ordinal

3

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language of work or name

English

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publication date

October 1989

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

86

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issue

20

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page(s)

7736-40

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Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 A resolution

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Crystal structure of rat intestinal fatty-acid-binding protein. Refinement and analysis of the Escherichia coli-derived protein with bound palmitate

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Crystallographic R factor refinement by molecular dynamics

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Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae

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Molecular dynamics simulations of the holo and apo forms of retinol binding protein. Structural and dynamical changes induced by retinol removal

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The structure of crystalline Escherichia coli-derived rat intestinal fatty acid-binding protein at 2.5-A resolution.

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Identification of a polypeptide growth inhibitor from bovine mammary gland. Sequence homology to fatty acid- and retinoid-binding proteins

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Protein crystallization by free interface diffusion

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Expression of rat intestinal fatty acid-binding protein in Escherichia coli. Purification and comparison of ligand binding characteristics with that of Escherichia coli-derived rat liver fatty acid-binding protein

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Identifiers

DOI

10.1073/PNAS.86.20.7736

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PubMed publication ID

2682622

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ResearchGate publication ID

20472856

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(Q27703753)

Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli

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