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| Home > Publications database > From Powder to Solution: Hemoglobin Dynamics Correlated to Body Temperature > print |
| 001 | 4704 | ||
| 005 | 20200402205616.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:19527667 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC2712052 |
| 024 | 7 | _ | |2 DOI |a 10.1016/j.bpj.2009.03.043 |
| 024 | 7 | _ | |2 WOS |a WOS:000267194600032 |
| 024 | 7 | _ | |2 MLZ |a Stadler2009 |
| 037 | _ | _ | |a PreJuSER-4704 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 100 | 1 | _ | |0 P:(DE-Juel1)VDB78506 |a Stadler, A.M. |b 0 |u FZJ |
| 245 | _ | _ | |a From Powder to Solution: Hemoglobin Dynamics Correlated to Body Temperature |
| 260 | _ | _ | |a New York, NY |b Rockefeller Univ. Press |c 2009 |
| 300 | _ | _ | |a 5073 - 5081 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 882 |a Biophysical Journal |v 96 |x 0006-3495 |y 12 |
| 500 | _ | _ | |a This work was supported by the European Commission under the 6th Framework Programme through the Key Action: Strengthening the European Research Area, Research Infrastructures (RII3-CT-2003-505925), the Institut Laue-Langevin (M.T.), and the AINSE (M.T.). |
| 520 | _ | _ | |a A transition in hemoglobin (Hb), involving partial unfolding and aggregation, has been shown previously by various biophysical methods. The correlation between the transition temperature and body temperature for Hb from different species, suggested that it might be significant for biological function. To focus on such biologically relevant human Hb dynamics, we studied the protein internal picosecond motions as a response to hydration, by elastic and quasielastic neutron scattering. Rates of fast diffusive motions were found to be significantly enhanced with increasing hydration from fully hydrated powder to concentrated Hb solution. In concentrated protein solution, the data showed that amino acid side chains can explore larger volumes above body temperature than expected from normal temperature dependence. The body temperature transition in protein dynamics was absent in fully hydrated powder, indicating that picosecond protein dynamics responsible for the transition is activated only at a sufficient level of hydration. A collateral result from the study is that fully hydrated protein powder samples do not accurately describe all aspects of protein picosecond dynamics that might be necessary for biological function. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK443 |2 G:(DE-HGF) |a Programm Biosoft |c N03 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Body Temperature |
| 650 | _ | 2 | |2 MeSH |a Elasticity |
| 650 | _ | 2 | |2 MeSH |a Hemoglobins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Neutrons |
| 650 | _ | 2 | |2 MeSH |a Powders |
| 650 | _ | 2 | |2 MeSH |a Solutions |
| 650 | _ | 2 | |2 MeSH |a Water: chemistry |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Hemoglobins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Powders |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Solutions |
| 650 | _ | 7 | |0 7732-18-5 |2 NLM Chemicals |a Water |
| 650 | _ | 7 | |2 WoSType |a J |
| 693 | _ | _ | |0 EXP:(DE-MLZ)TOF-TOF-20140101 |1 EXP:(DE-MLZ)FRMII-20140101 |5 EXP:(DE-MLZ)TOF-TOF-20140101 |6 EXP:(DE-MLZ)NL2au-20140101 |a Forschungs-Neutronenquelle Heinz Maier-Leibnitz |e TOFTOF: Cold neutron time-of-flight spectrometer |f NL2au |x 0 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Digel, I. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Embs, J.P. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Unruh, T. |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Zaccai, G. |b 4 |
| 700 | 1 | _ | |0 P:(DE-Juel1)131957 |a Büldt, G. |b 5 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Artmann, G. |b 6 |
| 773 | _ | _ | |0 PERI:(DE-600)1477214-0 |a 10.1016/j.bpj.2009.03.043 |g Vol. 96, p. 5073 - 5081 |p 5073 - 5081 |q 96<5073 - 5081 |t Biophysical journal |v 96 |x 0006-3495 |y 2009 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2712052 |
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| 914 | 1 | _ | |y 2009 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
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