TUHH Open Research
Help
  • Log In
    New user? Click here to register.Have you forgotten your password?
  • English
  • Deutsch
  • Communities & Collections
  • Publications
  • Research Data
  • People
  • Institutions
  • Projects
  • Statistics
  1. Home
  2. TUHH
  3. Publication References
  4. A combination of experiments and molecular dynamics simulation for the investigation of the ion-exchange adsorption of biological macromolecules
 
Options

A combination of experiments and molecular dynamics simulation for the investigation of the ion-exchange adsorption of biological macromolecules

Publikationstyp
Conference Paper
Date Issued
2013
Sprache
English
Author(s)
Liang, Juan  
Fieg, Georg  
Institut
Prozess- und Anlagentechnik V-4  
TORE-URI
http://hdl.handle.net/11420/7649
Start Page
25
End Page
30
Citation
23rd European Symposium on Computer Aided Process Engineering / ed. by Andrzej Kraslawski ... - Amsterdam [u.a.] : Elsevier [u.a.], 2013. - (Computer aided chemical engineering ; 32). - Seite 25-30
Contribution to Conference
23rd European Symposium on Computer Aided Process Engineering, ESCAPE 2013  
Publisher DOI
10.1016/B978-0-444-63234-0.50005-1
Scopus ID
2-s2.0-84879014355
Publisher
Elsevier
To get a comprehensive understanding of the adsorption of macromolecules onto ion-exchange adsorbent, the single component ion-exchange adsorptions of serum albumin and hemoglobin onto Q Sepharose FF were investigated with both adsorption equilibrium experiments and molecular dynamics (MD) simulations. Both of the investigations show that serum albumin adsorbs stronger than hemoglobin in the condition studied. The steric mass-action model was introduced to describe the adsorption equilibrium of both proteins, whose parameters were also studied with MD simulations. The results of MD simulations are qualitatively consistent with those of experiments.
Subjects
Hemoglobin
Ion-exchange adsorption
MD simulation
Serum albumin
SMA model
DDC Class
540: Chemie
660: Technische Chemie
TUHH
Weiterführende Links
  • Contact
  • Send Feedback
  • Cookie settings
  • Privacy policy
  • Impress
DSpace Software

Built with DSpace-CRIS software - Extension maintained and optimized by 4Science
Design by effective webwork GmbH

  • Deutsche NationalbibliothekDeutsche Nationalbibliothek
  • ORCiD Member OrganizationORCiD Member Organization
  • DataCiteDataCite
  • Re3DataRe3Data
  • OpenDOAROpenDOAR
  • OpenAireOpenAire
  • BASE Bielefeld Academic Search EngineBASE Bielefeld Academic Search Engine
Feedback