ArticleBiophysical journal2006
Structural and dynamical examination of the low-temperature glass transition in serum albumin.
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 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Structural origins of nitroxide side chain dynamics on membrane protein α-helical sites.Biochemistry · 2010Article
- Water molecule contributions to proton spin-lattice relaxation in rotationally immobilized proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
- Effects of surface water on protein dynamics studied by a novel coarse-grained normal mode approach.Biophysical journal · 2008Article
- Changes in protein structure and dynamics as a function of hydration from (1)H second moments.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2007Article
- Relaxation of protons by radicals in rotationally immobilized proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear magnetic transverse decay and the proton second moment of bovine serum albumin samples dry and hydrated with different water isotope compositions show that at temperatures around 170 K, there is a dramatic change in the dynamics of the water associated with the protein interface. By comparison, observation of the protein protons when hydrated with deuterium oxide provides no evidence for significant dynamical changes near 170 K. The proton second moment of the hydrated protein shows that the protein structure becomes more open with increasing hydration from the lyophilized condition and that the side chains extend from the protein surface into the solvent in the hydrated but not the dry cases. The proton second moment of serum albumin hydrated with H(2)O increases dramatically with decreasing temperature near 170 K, demonstrating that the water forms a rigid solid around the protein which effectively fills the surface irregularities created by the protein fold. Solvation with dimethyl sulfoxide yields small effects compared with water.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.