Use of Limited Proteolysis to Identify Protein Domains Suitable for Structural Analysis
- 1 January 2003
- book chapter
- Published by Elsevier
- Vol. 368, 77-84
- https://doi.org/10.1016/s0076-6879(03)68005-5
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Protein production: feeding the crystallographers and NMR spectroscopists.Nature Structural & Molecular Biology, 2000
- Structural proteomics of an archaeon.Nature Structural & Molecular Biology, 2000
- Structural proteomics: prospects for high throughput sample preparationProgress in Biophysics and Molecular Biology, 2000
- Elongin from Saccharomyces cerevisiaePublished by Elsevier ,2000
- Assessing annotation transfer for genomics: quantifying the relations between protein sequence, structure and function through traditional and probabilistic scoresJournal of Molecular Biology, 2000
- 100,000 protein structures for the biologistNature Structural & Molecular Biology, 1998
- A human cDNA encoding the 110-kDa A subunit of RNA polymerase II transcription factor elonginGene, 1996
- Elongin (SIII): A Multisubunit Regulator of Elongation by RNA Polymerase IIScience, 1995
- Overexpression, Purification, and Crystallization of the DNA Binding and Dimerization Domains of the Epstein-Barr Virus Nuclear Antigen 1Published by Elsevier ,1995
- Probing the solution structure of the DNA‐binding protein Max by a combination of proteolysis and mass spectrometryProtein Science, 1995