Literature DB >> 4218105

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

H L Crespi, A G Kostka, U H Smith.   

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Year:  1974        PMID： 4218105     DOI： 10.1016/s0006-291x(74)80440-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


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  4 in total

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

Authors:  D J Patel; L L Canuel
Journal:  Proc Natl Acad Sci U S A       Date:  1976-05       Impact factor: 11.205

2.  Sequence determination of reduction potentials by cysteinyl hydrogen bonds and peptide pipoles in [4Fe-4S] ferredoxins.

Authors:  B W Beck; Q Xie; T Ichiye
Journal:  Biophys J       Date:  2001-08       Impact factor: 4.033

3.  NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein.

Authors:  E Adman; K D Watenpaugh; L H Jensen
Journal:  Proc Natl Acad Sci U S A       Date:  1975-12       Impact factor: 11.205

4.  NMR studies of a complex of deuterated calmodulin with melittin.

Authors:  S H Seeholzer; M Cohn; J A Putkey; A R Means; H L Crespi
Journal:  Proc Natl Acad Sci U S A       Date:  1986-06       Impact factor: 11.205
  4 in total

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