Literature DB >> 5461769

Contribution of aromatic residue interactions to the stability of myoglobin. V. Enhancement by aromatic compounds of the rate of heat denaturation.

J R Cann, R L Cann.   

Abstract

Aromatic compounds like chlorpromazine and benzoate and its homologs strongly enhance the rate of heat denaturation of myoglobin. The latter apparently exert their action by complexing with a single kind of site in the hemeprotein. Both charge-transfer and hydrophobic interactions are implicated in complex formation, most probably with the heme moiety.

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Year:  1970        PMID: 5461769      PMCID: PMC1367754          DOI: 10.1016/S0006-3495(70)86302-0

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  4 in total

1.  Side-chain interactions in myoglobin.

Authors:  J C KENDREW
Journal:  Brookhaven Symp Biol       Date:  1962-12

2.  Contribution of aromatic residue interactions to the stability of myoglobin. IV. Delineation of binding forces between aromatic compounds and myoglobin.

Authors:  J R Cann
Journal:  Biochemistry       Date:  1969-10       Impact factor: 3.162

3.  Contribution of aromatic residue interactions to the stability of myoglobin. II. Enhancement by aromatic compounds of the rate of urea denaturation.

Authors:  J R Cann
Journal:  Biochemistry       Date:  1967-11       Impact factor: 3.162

4.  Contribution of aromatic residue interactions to the stability of myoglobin. 3. Molecular complexes of aromatic compounds with hemin, hematoporphyrin, and myoglobin.

Authors:  J R Cann
Journal:  Biochemistry       Date:  1967-11       Impact factor: 3.162

  4 in total
  1 in total

Review 1.  Mass Spectrometry Methods for Measuring Protein Stability.

Authors:  Daniel D Vallejo; Carolina Rojas Ramírez; Kristine F Parson; Yilin Han; Varun V Gadkari; Brandon T Ruotolo
Journal:  Chem Rev       Date:  2022-03-22       Impact factor: 72.087

  1 in total

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