ArticleBiophysical journal2006
Low-temperature glass transitions of quenched and annealed bovine serum albumin aqueous solutions.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 65 citations in OpenAlex.
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- Vitrification Solutions for Plant Cryopreservation: Modification and Properties.Plants (Basel, Switzerland) · 2021Review
- Observation of Microstructure Formation During Freeze-Drying of Dextrin Solution byFrontiers in chemistry · 2018Article
- Analysis of Interaction Between Interfacial Structure and Fibrinogen at Blood-Compatible Polymer/Water Interface.Frontiers in chemistry · 2018Article
- Low-temperature polymorphic phase transition in a crystalline tripeptide L-Ala-L-Pro-Gly·H2O revealed by adiabatic calorimetry.The journal of physical chemistry. B · 2015Article
- Structural and dynamical examination of the low-temperature glass transition in serum albumin.Biophysical journal · 2006Article
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To investigate the glass transition behaviors of a 20% (w/w) aqueous solution of bovine serum albumin, heat capacities and enthalpy relaxation rates were measured by adiabatic calorimetry at temperatures ranging from 80 to 300 K. One series of measurements was carried out after quenching from 300 down to 80 K and another after annealing in 200-240 K. The quenched sample showed a heat capacity jump indicating a glass transition temperature T(g) = 170 K, and the annealed sample showed a smaller jump with the T(g) shifted toward the higher temperature side. The temperature dependence of the enthalpy relaxation rates for the quenched sample indicated the presence of two enthalpy relaxation effects: one at around 110 K and the other over a wide temperature range (120-190 K). The annealed sample showed three separate relaxation effects giving 1) T(g) = 110 K, 2) 135 K, and 3) temperature higher than 180 K, whereas nothing around 170 K. These effects were thought to originate, respectively, from the rearrangement motions of 1) primary hydrate water forming a direct hydrogen bond with the protein, 2) part of the internal water localized in the opening of a protein structure, and 3) the disordered region in the protein.
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