An experimental approach to probe conformational changes in proteinstructure using a biotin derivative followed by mass spectrometry

An experimental approach to probe conformational changes in proteinstructure using a biotin derivative followed by mass spectrometry

The biotinylation patterns of two soluble model proteins (BSA and CA II) were analyzed under different conditions. In a first step these proteins were biotinylated with an increasing molar excess of a biotin derivative. In this case increases in biotin concentration led to an increase in the number...

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Bibliographic Details
Main Author: Azimzadeh, Omid
Contributors: Lingelbach, Klaus (Prof. Dr. ) (Thesis advisor)
Format: Doctoral Thesis
Language:English
Published: Philipps-Universität Marburg 2008
Subjects:
Biotinylierung
Mass spectrometry
Biowissenschaften, Biologie
Massenspektrometrie
Bovines Serum Albumin
Konformationsänderung
Biotinylation
Plasmodium falciparum
Conformational changes
Bovine serum albumin
Life sciences
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Call Number: urn:nbn:de:hebis:04-z2008-07477
Publication Date: 2008-11-24
Date of Acceptance: 2008-10-27
Source: Use of Biotin Derivatives to Probe Conformational Changes, July 27, 2007, VOL. 282, NO. 30, pp. 21609–21617
Downloads: 29 (2023), 29 (2022), 46 (2021), 40 (2020), 151 (2019), 56 (2018)
License: https://rightsstatements.org/vocab/InC-NC/1.0/
Access URL: https://archiv.ub.uni-marburg.de/diss/z2008/0747
https://doi.org/10.17192/z2008.0747

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