(Q70997083)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8599759%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

title

Pseudocontact shifts used in the restraint of the solution structures of electron transfer complexes (English)

1 reference

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15 October 2019

author name string

Guiles RD

1

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15 October 2019

Sarma S

2

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15 October 2019

DiGate RJ

3

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15 October 2019

Banville D

4

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15 October 2019

Basus VJ

5

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15 October 2019

Kuntz ID

6

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15 October 2019

Waskell L

7

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15 October 2019

publication date

1 April 1996

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Nature structural biology

15 October 2019

published in

1 reference

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15 October 2019

volume

3

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15 October 2019

issue

4

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15 October 2019

page(s)

333-339

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Long-range electron transfer in heme proteins

15 October 2019

cites work

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Comparison of theory and experiment for electron transfers in proteins: where's the beef?

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Three-dimensional Fourier synthesis of calf liver cytochrome b 5 at 2-8 A resolution

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An hypothetical structure for an intermolecular electron transfer complex of cytochromes c and b5

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Molecular dynamics of a cytochrome c-cytochrome b5 electron transfer complex

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Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5

31 March 2020

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Electrostatic analysis of the interaction of cytochrome c with native and dimethyl ester heme substituted cytochrome b5

31 March 2020

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Probing the mechanisms of macromolecular recognition: the cytochrome b5-cytochrome c complex

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Crosslinking of cytochrome c and cytochrome b5 with a water-soluble carbodiimide. Reaction conditions, product analysis and critique of the technique

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Structural studies of cytochrome b5: complete sequence-specific resonance assignments for the trypsin-solubilized microsomal ferrocytochrome b5 obtained from pig and calf

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An analysis of pseudocontact shifts and their relationship to structural features of the redox states of cytochrome b5.

31 March 2020

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Sequence-specific 1H and 15N resonance assignments for both equilibrium forms of the soluble heme binding domain of rat ferrocytochrome b5.

31 March 2020

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Novel heteronuclear methods of assignment transfer from a diamagnetic to a paramagnetic protein: application to rat cytochrome b5.

31 March 2020

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Proton resonance assignments of horse ferricytochrome c

31 March 2020

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Comparison of the solution and crystal structures of mitochondrial cytochrome c. Analysis of paramagnetic shifts in the nuclear magnetic resonance spectrum of ferricytochrome c.

31 March 2020

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1H-n.m.r. investigation of the interaction between cytochrome c and cytochrome b5.

31 March 2020

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

31 March 2020

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Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution

31 March 2020

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Isotope-edited proton NMR study on the structure of a pepsin/inhibitor complex

31 March 2020

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Synthesis, bacterial expression, and mutagenesis of the gene coding for mammalian cytochrome b5.

31 March 2020

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[21] Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction

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31 March 2020

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31 March 2020

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1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5.

31 March 2020

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Molecular dynamics simulation of cytochrome b5: implications for protein-protein recognition

31 March 2020

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NMR determination of the orientation of the magnetic susceptibility tensor in cyanometmyoglobin: a new probe of steric tilt of bound ligand

31 March 2020

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Use of lanthanide-induced nuclear magnetic resonance shifts for determination of protein structure in solution: EF calcium binding site of carp parvalbumin

31 March 2020

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Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSB0496-333

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:8599759%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

1 reference