ArticleBiophysical journal2007
Multiphasic kinetics of myoglobin/sodium dodecyl sulfate complex formation.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Fibrillation/defibrillation of myoglobin decorated with gold nanoparticles probed through nanometal surface energy transfer mechanism.RSC advances · 2026Article
- Modification of Whey Protein Isolate with Surfactants Based on Hofmeister Series and Interaction Parameter.ACS omega · 2026Article
- Kinetics of Structural Transitions Induced by Sodium Dodecyl Sulfate in α-Chymotrypsin.ACS omega · 2023Article
- The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes: Effect on structure and catalysis.Journal of inorganic biochemistry · 2019Article
- Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes.Biochemistry · 2018Article
- Denaturation of proteins by SDS and tetraalkylammonium dodecyl sulfates.Langmuir : the ACS journal of surfaces and colloids · 2011Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have carried out a kinetic analysis of the conformational changes that myoglobin (Mb) undergoes in the presence of the anionic surfactant sodium dodecyl sulfate (SDS). The time-resolved results have been combined with steady-state circular dichroism (CD) and resonance Raman (RR) spectroscopy. Time-resolved absorption spectra indicate that SDS induces changes in the heme coordination with the formation of three different Mb species, depending on SDS concentration. The formation of the Mb/SDS complex involves three or four phases, depending on surfactant concentration. The kinetic data are analyzed assuming two modes of interaction according to whether SDS is monomeric or micellar. The two pathways are separated but interconnected through free Mb. At the lowest concentrations a six-coordinated, low-spin form dominates. Two distinct five-coordinated species are formed at higher SDS concentrations: one is a protein-free heme and the other reequilibrates slowly with the six-coordinated, low-spin form. The resulting complexes have been characterized by CD and RR. In addition, CD spectra show that the local changes in the heme environment are coupled to changes in the protein structure.
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Registered trials
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