Hochschulschrift
Structural characterization of chaperone assisted folding and assembly of RuBisCO
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Dimensions
-
30 cm
- Extent
-
IV, 146 S.
- Language
-
Englisch
- Notes
-
Ill., graph. Darst.
München, Univ., Diss., 2009
- Keyword
-
Oxidoreductasen
Reductasen
Molekülstruktur
Strukturbiologie
- Creator
- Table of contents
- Rights
-
Bei diesem Objekt liegt nur das Inhaltsverzeichnis digital vor. Der Zugriff darauf ist unbeschränkt möglich.
- Last update
- 11.06.2025, 1:45 PM CEST
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
Other Objects (12)
Structural characterization of chaperone assisted folding and assembly of RuBisCO
Chaperone assisted RuBisCO folding and assembly-role of RbcX
Folding and assembly of RuBisCO : structural and functional characterization of the RuBisCO assembly chaperone RbcX
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Resolving chaperone-assisted protein folding on the ribosome at the peptide level
Interactions driving Chaperone-assisted Assembly of Proteasome Core particles
Tracking chaperone-mediated folding using force spectroscopy
Analysis of chaperone function in multi-domain protein folding
Folding and assembly of antibodies
Chaperone solvent-assisted assembly of polymers at the interface of two immiscible liquids
The cumulative impact of chaperone mediated protein-folding during evolution
The cumulative impact of chaperone mediated protein- folding during evolution
Structural characterization of chaperone assisted folding and assembly of RuBisCO
Chaperone assisted RuBisCO folding and assembly-role of RbcX
Folding and assembly of RuBisCO : structural and functional characterization of the RuBisCO assembly chaperone RbcX
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Resolving chaperone-assisted protein folding on the ribosome at the peptide level
Interactions driving Chaperone-assisted Assembly of Proteasome Core particles
Tracking chaperone-mediated folding using force spectroscopy
Analysis of chaperone function in multi-domain protein folding
Folding and assembly of antibodies
Chaperone solvent-assisted assembly of polymers at the interface of two immiscible liquids
The cumulative impact of chaperone mediated protein-folding during evolution
The cumulative impact of chaperone mediated protein- folding during evolution
Structural characterization of chaperone assisted folding and assembly of RuBisCO
Chaperone assisted RuBisCO folding and assembly-role of RbcX
Folding and assembly of RuBisCO : structural and functional characterization of the RuBisCO assembly chaperone RbcX
Chaperone-assisted folding of newly synthesized proteins in the cytosol
Resolving chaperone-assisted protein folding on the ribosome at the peptide level
Interactions driving Chaperone-assisted Assembly of Proteasome Core particles
Tracking chaperone-mediated folding using force spectroscopy
Analysis of chaperone function in multi-domain protein folding
Folding and assembly of antibodies
Chaperone solvent-assisted assembly of polymers at the interface of two immiscible liquids
The cumulative impact of chaperone mediated protein-folding during evolution