- Alternative title
-
Mechanochemie von Disulfidbrücken in Proteinen
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Heidelberg, Universität Heidelberg, Dissertation, 2013
- Keyword
-
Proteins
Bonds
Mechanical chemistry
Von Willebrand factor
Thioredoxin
Biomechanik
Biodynamik
- Event
-
Veröffentlichung
- (where)
-
Heidelberg
- (who)
-
Universitätsbibliothek Heidelberg
- (when)
-
2013
- Creator
- Contributor
-
Comba, Peter
- DOI
-
10.11588/heidok.00014398
- URN
-
urn:nbn:de:bsz:16-heidok-143984
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:48 PM CET
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Object type
- Hochschulschrift
Associated
- Baldus, Ilona Beatrice
- Comba, Peter
- Universitätsbibliothek Heidelberg
Time of origin
- 2013
Other Objects (12)
Mechanochemistry of disulfide bonds in proteins
Synthesis and biological evaluation of complex peptides containing disulfide bonds
Redox regulation of Annexin A1 : structural and functional requirement of disulfide bonds
Molecular insights into the protein disulfide isomerase family
Molecular insights into the protein disulfide isomerase family
A structural disulfide bond ín the mitochondrial ΤΙΜ23 translocase is critical for voltage gating and efficient protein import
Role of protein disulfide isomerase for activation of blood coagulation by atherosclerotic plaques
Mapping disulfide bonds and free sulfides in the small hepatitis B envelope protein S
Protein disulfide isomerase extracellular adherence protein cooperatively potentiate staphylococcal invasion into endothelial cells
Mechanisms of novel thiol-disulfide oxidoreductases
Molecular dimer junctions forming: Role of disulfide bonds and electrode-compression-time
Disulfide Bond Engineering of an Endoglucanase from Penicillium verruculosum to Improve Its Thermostability
Mechanochemistry of disulfide bonds in proteins
Synthesis and biological evaluation of complex peptides containing disulfide bonds
Redox regulation of Annexin A1 : structural and functional requirement of disulfide bonds
Molecular insights into the protein disulfide isomerase family
Molecular insights into the protein disulfide isomerase family
A structural disulfide bond ín the mitochondrial ΤΙΜ23 translocase is critical for voltage gating and efficient protein import
Role of protein disulfide isomerase for activation of blood coagulation by atherosclerotic plaques
Mapping disulfide bonds and free sulfides in the small hepatitis B envelope protein S
Protein disulfide isomerase extracellular adherence protein cooperatively potentiate staphylococcal invasion into endothelial cells
Mechanisms of novel thiol-disulfide oxidoreductases
Molecular dimer junctions forming: Role of disulfide bonds and electrode-compression-time
Disulfide Bond Engineering of an Endoglucanase from Penicillium verruculosum to Improve Its Thermostability
Mechanochemistry of disulfide bonds in proteins
Synthesis and biological evaluation of complex peptides containing disulfide bonds
Redox regulation of Annexin A1 : structural and functional requirement of disulfide bonds
Molecular insights into the protein disulfide isomerase family
Molecular insights into the protein disulfide isomerase family
A structural disulfide bond ín the mitochondrial ΤΙΜ23 translocase is critical for voltage gating and efficient protein import
Role of protein disulfide isomerase for activation of blood coagulation by atherosclerotic plaques
Mapping disulfide bonds and free sulfides in the small hepatitis B envelope protein S
Protein disulfide isomerase extracellular adherence protein cooperatively potentiate staphylococcal invasion into endothelial cells
Mechanisms of novel thiol-disulfide oxidoreductases
Molecular dimer junctions forming: Role of disulfide bonds and electrode-compression-time