(Q41861339)

13 October 2017

Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study (English)

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13 October 2017

Rhodobacter capsulatus

object named as

Rhodobacter capsulatus

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1

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13 October 2017

D Zhao

2

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PubMed ID

1668720

13 October 2017

N E MacKenzie

series ordinal

3

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13 October 2017

1 July 1991

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Journal of Biomolecular NMR

13 October 2017

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13 October 2017

1

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13 October 2017

2

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13 October 2017

145-154

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https://scigraph.springernature.com/pub.10.1007/bf01877226

13 October 2017

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cites work

Identification of an allosterically sensitive unfolding unit in hemoglobin

1 reference

12 December 2020

Conformation change of cytochrome c. II. Ferricytochrome c refinement at 1.8 A and comparison with the ferrocytochrome structure

1 reference

12 December 2020

Hydrogen Exchange in Proteins

1 reference

12 December 2020

Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.

1 reference

12 December 2020

A spectroscopic analysis of the Pro35 Ala mutant of Rhodobacter capsulatus cytochrome c2. The strictly conserved Pro35 is not structurally essential

1 reference

12 December 2020

Primary structure effects on peptide group hydrogen exchange.

1 reference

12 December 2020

Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance

1 reference

12 December 2020

Two-dimensional 1H NMR studies of cytochrome c: hydrogen exchange in the N-terminal helix

1 reference

12 December 2020

High-resolution three-dimensional structure of horse heart cytochrome c

1 reference

12 December 2020

Effects of Nonpolar Environments on the Redox Potentials of Heme Complexes

1 reference

12 December 2020

Hydrogen exchange and structural dynamics of proteins and nucleic acids

1 reference

12 December 2020

Pro → Ala-35 Rhodobacter capsulatus cytochrome c 2 shows dynamic not structural differences

1 reference

12 December 2020

Exchange behavior of the H-bonded amide protons in the 3 to 13 helix of ribonuclease S

1 reference

12 December 2020

High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c

1 reference

12 December 2020

Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution

1 reference

12 December 2020

Assignment of the 1H and 15N NMR spectra of Rhodobacter capsulatus ferrocytochrome c2

1 reference

12 December 2020

Identifiers

DOI

10.1007/BF01877226

1 reference

PubMed ID

1668720

Dimensions Publication ID

13 October 2017

0 references

1 reference

PubMed ID

1668720