Journal Article FZJ-2016-07473

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Protein Entrapment in Polymeric Mesh: Diffusion in Crowded Environment with Fast Process on Short Scales

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2016
Soc. Washington, DC

Macromolecules 49(5), 1941 - 1949 () [10.1021/acs.macromol.5b02281]

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Abstract: The natural environment of proteins is a crowded environment as in cells, extracellular fluids, or during processing. Semidilute polymer solutions have been a source of rich structural and dynamical properties and mimic a crowded environment, but a proper understanding of protein dynamics in the crowded environment is far lagging. Such a study not only realizes protein’s natural environment in a crowded solution in the cell or during processing but also manifests the underlying protein–polymer interaction. By dispersing model globular proteins like α-lactalbumin (La) and hemoglobin (Hb), in aqueous solution of poly(ethylene oxide) (PEO) we mimic a crowded environment and use state-of-the-art neutron spin echo (NSE) and small-angle neutron scattering (SANS) techniques to observe the corresponding protein dynamics in semidilute polymer solution. NSE can access the fast diffusion process (Dfast) prior to the slow diffusion process on long times and length scales (Dγ). The protein dynamics in a crowded environment can be described analogous to the diffusion in a periodic potential. The fast dynamics corresponds to diffusion inside a trap built by the polymer mesh while the slower process is the long time diffusion on macroscopic length scales also observed by other techniques. We observe the onset of fractional diffusion for higher concentrated polymer solutions.

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Contributing Institute(s):
  1. Neutronenstreuung (ICS-1)
  2. Neutronenstreuung (Neutronenstreuung ; JCNS-1)
  3. JCNS-SNS (JCNS-SNS)
  4. Streumethoden (JCNS-2)
Research Program(s):
  1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)
  2. 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623) (POF3-623)
  3. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)

Appears in the scientific report 2016
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Medline ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; NationallizenzNationallizenz ; No Authors Fulltext ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection
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Dokumenttypen > Aufsätze > Zeitschriftenaufsätze
Institutssammlungen > JCNS > JCNS-SNS
Institutssammlungen > JCNS > JCNS-2
Institutssammlungen > JCNS > JCNS-1
Institutssammlungen > IBI > IBI-8
Workflowsammlungen > Öffentliche Einträge
ICS > ICS-1
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 Datensatz erzeugt am 2016-12-13, letzte Änderung am 2024-06-19


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