• Deutsch
    • English
  • English 
    • Deutsch
    • English
  • Login
Item View 
  •   Home
  • Zentren & Graduiertenschulen
  • GGNB - Göttinger Graduiertenzentrum für Neurowissenschaften, Biophysik und molekulare Biowissenschaften
  • Item View
  •   Home
  • Zentren & Graduiertenschulen
  • GGNB - Göttinger Graduiertenzentrum für Neurowissenschaften, Biophysik und molekulare Biowissenschaften
  • Item View
JavaScript is disabled for your browser. Some features of this site may not work without it.

Paramagnetic tools for the structural analysis of high molecular weight proteins

by Aldo Roman Camacho Zarco
Doctoral thesis
Date of Examination:2015-01-19
Date of issue:2015-12-10
Advisor:Prof. Dr. Markus Zweckstetter
Referee:Prof. Dr. Marina Bennati
Referee:Prof. Dr. Ralph Kehlenbach
Referee:Prof. Dr. Claudia Höbartner
crossref-logoPersistent Address: http://dx.doi.org/10.53846/goediss-5421

 

 

Files in this item

Name:AldoOptimized.pdf
Size:2.88Mb
Format:PDF
ViewOpen

The following license files are associated with this item:


Abstract

English

   Paramagnetic effects provide important structural and dynamic information of biomolecules. However, the attachment of lanthanides through small chelating organic molecules to proteins (the most common way to obtain paramagnetic effects) requires single cysteine mutants, optimization of the tagging reaction and previous knowledge of the three-dimensional structure of the target to select proper attachment sites. In this work was developed a new method that relieves most of these disadvantages: the lanthanide is not directly attached to the target protein, but instead to a "reporter" protein that binds and transmits paramagnetic information to the target protein.     In this thesis is shown that the attachment of a lanthanide in different locations on the surface of the reporter protein PDZ allows measuring residual dipolar couplings and pseudo contact shifts from several independent molecular alignments on any target. This is shown for ubiquitin and the maltose binding protein. The fusion of a 7-residue PDZ recognition peptide to the C-terminus of the target proteins is the only necessary modification to obtain the paramagnetic restraints. Therefore, this method allows recording a large amount of paramagnetic information from orientationally independent molecular alignments in proteins. Moreover, it is not necessary to have previous knowledge of the three-dimensional structure of the targets.
Keywords: NMR spectroscopy; Lanthanides; Proteins; Structural restraints
 

Statistik

Publish here

Browse

All of eDissFaculties & ProgramsIssue DateAuthorAdvisor & RefereeAdvisorRefereeTitlesTypeThis FacultyIssue DateAuthorAdvisor & RefereeAdvisorRefereeTitlesType

Help & Info

Publishing on eDissPDF GuideTerms of ContractFAQ

Contact Us | Impressum | Cookie Consents | Data Protection Information | Accessibility
eDiss Office - SUB Göttingen (Central Library)
Platz der Göttinger Sieben 1
Mo - Fr 10:00 – 12:00 h


Tel.: +49 (0)551 39-27809 (general inquiries)
Tel.: +49 (0)551 39-28655 (open access/parallel publications)
ediss_AT_sub.uni-goettingen.de
[Please replace "_AT_" with the "@" sign when using our email adresses.]
Göttingen State and University Library | Göttingen University
Medicine Library (Doctoral candidates of medicine only)
Robert-Koch-Str. 40
Mon – Fri 8:00 – 24:00 h
Sat - Sun 8:00 – 22:00 h
Holidays 10:00 – 20:00 h
Tel.: +49 551 39-8395 (general inquiries)
Tel.: +49 (0)551 39-28655 (open access/parallel publications)
bbmed_AT_sub.uni-goettingen.de
[Please replace "_AT_" with the "@" sign when using our email adresses.]