Literature DB >> 5721

Nuclear magnetic resonance studies of slowly exchanging peptide protons in cytochrome c in aqueous solution.

D J Patel, L L Canuel.   

Abstract

The slowly exchanging protons in oxidized and reduced horse heart cytochrome c (D20, uncorrected pH meter reading 6.5 room temperature) have been monitored by recording the 270 and 360 MHz proton nuclear magnetic resonance spectra of the reduced protein between 5 and 11 parts per million downfield from 2,2-dimethyl-2-silapentane-5-sulfonate.

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Year:  1976        PMID： 5721      PMCID： PMC430301          DOI： 10.1073/pnas.73.5.1398

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  23 in total

1.  Assignment of aromatic amino acid PMR resonances of horse ferrocytochrome C.

Authors:  G R Moore; R J Williams
Journal:  FEBS Lett       Date:  1975-05-15       Impact factor: 4.124

2.  Studies of exchangeable hydrogens in lysozyme by means of Fourier transform proton magnetic resonance.

Authors:  I D Campbell; C M Dobson; J P Williams
Journal:  Proc R Soc Lond B Biol Sci       Date:  1975-06-17

3.  Assignment of aromatic amino acid PMR resonances of horse ferricytochrome c.

Authors:  C M Dobson; G R Moore; R J Williams
Journal:  FEBS Lett       Date:  1975-03-01       Impact factor: 4.124

4.  Nuclear magnetic resonance study of exchangeable protons in ferrocytochrome c.

Authors:  E Stellwagen; R G Shulman
Journal:  J Mol Biol       Date:  1973-04-25       Impact factor: 5.469

5.  Proton magnetic resonance studies of horse cytochrome c.

Authors:  C C McDonald; W D Phillips
Journal:  Biochemistry       Date:  1973-08-14       Impact factor: 3.162

6.  Biologically important isotope hybrid compounds in NMR: 1 H fourier transform NMR at unnatural abundance.

Authors:  J J Katz; H L Crespi
Journal:  Pure Appl Chem       Date:  1972       Impact factor: 2.453

7.  Conformational changes upon reduction of cytochrome c.

Authors:  T Takano; R Swanson; O B Kallai; R E Dickerson
Journal:  Cold Spring Harb Symp Quant Biol       Date:  1972

8.  Pulsed NMR study of the structure of cytochrome c.

Authors:  A G Redfield; R K Gupta
Journal:  Cold Spring Harb Symp Quant Biol       Date:  1972

9.  Hydrogen-tritium exchange in polypeptides. Models of alpha-helical and beta conformations.

Authors:  W H Welch; G D Fasman
Journal:  Biochemistry       Date:  1974-06-04       Impact factor: 3.162

10.  Proton Magnetic resonance observations of hydrogen exchange rates and secondary structure in algal ferredoxin.

Authors:  H L Crespi; A G Kostka; U H Smith
Journal:  Biochem Biophys Res Commun       Date:  1974-12-23       Impact factor: 3.575
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  5 in total

Review 1.  Protein compressibility, dynamics, and pressure.

Authors:  D P Kharakoz
Journal:  Biophys J       Date:  2000-07       Impact factor: 4.033

2.  Increase in apparent compressibility of cytochrome c upon oxidation.

Authors:  D Eden; J B Matthew; J J Rosa; F M Richards
Journal:  Proc Natl Acad Sci U S A       Date:  1982-02       Impact factor: 11.205

3.  Insights into the alkaline transformation of ferricytochrome c from (1)H NMR studies in 30% acetonitrile-water.

Authors:  S G Sivakolundu; P A Mabrouk
Journal:  Protein Sci       Date:  2001-11       Impact factor: 6.725

4.  Differences in hydrogen exchange behavior between the oxidized and reduced forms of Escherichia coli thioredoxin.

Authors:  S M Kaminsky; F M Richards
Journal:  Protein Sci       Date:  1992-01       Impact factor: 6.725

5.  Amide proton exchange rates of oxidized and reduced Saccharomyces cerevisiae iso-1-cytochrome c.

Authors:  J L Marmorino; D S Auld; S F Betz; D F Doyle; G B Young; G J Pielak
Journal:  Protein Sci       Date:  1993-11       Impact factor: 6.725
  5 in total

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