15N-labelling and preliminary heteronuclear NMR study ofDesulfovibrio vulgaris Hildenborough cytochrome c553

about

Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state Mapping the cytochrome c 553 interacting site using 1 H and 15 N NMR

P2860

Q27625056-E08151C0-0D85-40C2-99A9-F80EDC8BABFC Q57965098-A7EF6850-343E-47B9-8743-86F877DE720D

P2860

15N-labelling and preliminary heteronuclear NMR study ofDesulfovibrio vulgaris Hildenborough cytochrome c553

Item

http://www.wikidata.org/entity/Q57965102

description

im April 1999 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published on 01 April 1999

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована у квітні 1999

@uk

name

15N-labelling and preliminary ...... Hildenborough cytochrome c553

@en

15N-labelling and preliminary ...... Hildenborough cytochrome c553

@nl

type

Item

label

15N-labelling and preliminary ...... Hildenborough cytochrome c553

@en

15N-labelling and preliminary ...... Hildenborough cytochrome c553

@nl

prefLabel

15N-labelling and preliminary ...... Hildenborough cytochrome c553

@en

15N-labelling and preliminary ...... Hildenborough cytochrome c553

@nl

P1476

15N-labelling and preliminary ...... Hildenborough cytochrome c553

@en

P2093

A Dolla

http://www.w3.org/2001/XMLSchema#string

F Guerlesquin

http://www.w3.org/2001/XMLSchema#string

R Toci

http://www.w3.org/2001/XMLSchema#string

P2860

Structure and dynamics of ferrocytochrome c553 from Desulfovibrio vulgaris studied by NMR spectroscopy and restrained molecular dynamics

Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins

Protein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c.

Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough.

Functional expression of Desulfovibrio vulgaris Hildenborough cytochrome c3 in Desulfovibrio desulfuricans G200 after conjugational gene transfer from Escherichia coli.

Cytochrome c550 from Thiobacillus versutus: cloning, expression in Escherichia coli, and purification of the heterologous holoprotein.

The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins.

P304

398-404

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1046/J.1432-1327.1999.00292.X

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

261

http://www.w3.org/2001/XMLSchema#string

P50

Xavier Morelli

P577

1999-04-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

10215849

http://www.w3.org/2001/XMLSchema#string

15N-labelling and preliminary heteronuclear NMR study ofDesulfovibrio vulgaris Hildenborough cytochrome c553

about

P2860

P2860

15N-labelling and preliminary heteronuclear NMR study ofDesulfovibrio vulgaris Hildenborough cytochrome c553

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698