Logo der Universität Basel

Research Database / FORSCHUNGSDATENBANK 
PRINTDOC
 
Publication 155475 | Verified
 

Data Entry: Please note that the research database will be replaced by UNIverse by the end of October 2023. Please enter your data into the system https://universe-intern.unibas.ch. Thanks

Login for users with Unibas email account...

Login for registered users without Unibas email account...

 
Aggregation of linear biopolymers induced by cooperative binding of ligands
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 155475
Author(s) Schwarz, G; Seelig-Löffler, A
Author(s) at UniBasel Seelig-Löffler, Anna
Year 1975
Title Aggregation of linear biopolymers induced by cooperative binding of ligands
Journal Biochimica et biophysica acta
Volume 379
Number 1
Pages / Article-Number 125-38
Keywords *Acridines; Binding Sites; Biopolymers; Glutamates; Kinetics; Mathematics; Models; Chemical; Molecular Weight; *Peptides; *Protein Binding; Scattering; Radiation; Temperature; Thermodynamics
Abstract Owing to "stacking" interactions certain positively charged dye molecules display biologically significant cooperative binding to single stranded polyanions. Temperature jump experiments with such systems reveal a peculiar slow relaxation process which cannot be ascribed to the actual binding reactions. In the special case of poly(glutamic acid) and acridine orange, light scattering measurements show it to be caused by a strong aggregation of the polymer-dye complexes depending primarily on the degree of binding. This effect is clearly reflected in changes of the visible absorption spectrum. Their wavelength dependences indicate that the aggregation is apparently associated with a spectral flattening as well as an enhanced binding of the dye which both result in a decrease of its absorbance. The thermodynamics and kinetics of the phenomenon can be understood on the basis of a simple model.
Publisher Elsevier
ISSN/ISBN 0006-3002
edoc-URL http://edoc.unibas.ch/dok/A5258503
Full Text on edoc No
Digital Object Identifier DOI 10.1016/0005-2795(75)90014-8
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/1115791
ISI-Number WOS:A1975V527100013
Document type (ISI) Article
 
   

MCSS v5.8 PRO. 0.523 sec, queries - 0.000 sec ©Universität Basel  |  Impressum   |    
24/04/2024