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Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy

Kavak Balci, Gulten


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{
  "DOI": "10.1007/s10953-021-01052-z", 
  "abstract": "In this work, the proton spin-lattice (T-1) and spin-spin (T-2) relaxation times of aqueous solutions of bovine serum albumin (BSA) were investigated as a function of temperature. The T-1 relaxation times were measured versus temperature (T) for five H2O solutions containing different BSA concentrations. The sample temperature was varied from 304 to 253 K for each concentration. T-2 measurements were carried out versus the BSA concentrations only. The least-square fitting of ln(T-1) versus T-1 yields a linear correlation. The effective correlation times tau(1) for T-1 and tau(2) for T-2 were calculated by using experimental data and the related theory. The data suggest that surface water is responsible for the dipolar relaxation mechanisms. Both T-1 and T-2 mechanisms are caused by overall tumbling of albumin molecule causing the rotational correlation time. However, some slow motions may contribute to the T-2 mechanism.", 
  "author": [
    {
      "family": "Kavak Balci", 
      "given": " Gulten"
    }
  ], 
  "container_title": "JOURNAL OF SOLUTION CHEMISTRY", 
  "id": "236362", 
  "issue": "2", 
  "issued": {
    "date-parts": [
      [
        2021, 
        1, 
        1
      ]
    ]
  }, 
  "page": "232-239", 
  "title": "Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy", 
  "type": "article-journal", 
  "volume": "50"
}
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Kavak Balci, G. (2021). Investigation of Temperature Dependence of Protein Solutions by NMR Spectroscopy. JOURNAL OF SOLUTION CHEMISTRY, 50(2), 232–239. doi:10.1007/s10953-021-01052-z

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