(Q44291705)

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High specificity of a phosphate transport protein determined by hydrogen bonds

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1 December 2017

High specificity of a phosphate transport protein determined by hydrogen bonds (English)

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Europe PubMed Central

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1 December 2017

author name string

H Luecke

1

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1 December 2017

F A Quiocho

2

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1 December 2017

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publication date

1 September 1990

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1 December 2017

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1 December 2017

347

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1 December 2017

6291

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1 December 2017

402-406

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1 December 2017

Phosphate transport in Escherichia coli

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Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria.

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Structural gene for the phosphate-repressible phosphate-binding protein of Escherichia coli has its own promoter: complete nucleotide sequence of the phoS gene

1 reference

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Resolution of phase ambiguity in macromolecular crystallography

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Improved Fourier coefficients for maps using phases from partial structures with errors

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Crystallographic R factor refinement by molecular dynamics

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Stereochemically restrained refinement of macromolecular structures

1 reference

https://api.crossref.org/works/10.1038%2F347402A0

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Carboxyl-carboxylate interactions in proteins

1 reference

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Sulfate-binding protein dislikes protonated oxyacids. A molecular explanation

1 reference

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Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds

1 reference

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The 2 A resolution structure of the sulfate-binding protein involved in active transport in Salmonella typhimurium

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Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units

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Structure and function of voltage-sensitive ion channels

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An all atom force field for simulations of proteins and nucleic acids

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Identifiers

10.1038/347402A0

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Europe PubMed Central

PubMed publication ID

1 December 2017

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PubMed publication ID

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Europe PubMed Central

PubMed publication ID

1 December 2017

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