Conformational states of aspartate transcarbamoylase stabilized with a cross-linking reagent.
Open Access
- 1 August 1979
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 254 (13) , 6180-6186
- https://doi.org/10.1016/s0021-9258(18)50535-4
Abstract
No abstract availableThis publication has 27 references indexed in Scilit:
- Freezing of dCMP aminohydrolase in the activated conformation by glutaraldehydeJournal of Molecular Biology, 1978
- Refinement of the Coomassie blue method of protein quantitationAnalytical Biochemistry, 1978
- Allosteric regulation of aspartate transcarbamoylase. Analysis of the structural and functional behavior in terms of a two-state modelBiochemistry, 1977
- The use of a new series of cleavable protein‐crosslinkers on the Escherichia coli ribosomeFEBS Letters, 1974
- An aspartate transcarbamylase lacking catalytic subunit interactions: II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactionsJournal of Molecular Biology, 1973
- Conformational changes in proteins as measured by difference sedimentation studies. II. Effect of stereospecific ligands on the catalytic subunit of aspartate transcarbamylaseBiochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- New Structural Model of E. coli Aspartate Transcarbamylase and the Amino-acid Sequence of the Regulatory Polypeptide ChainNature, 1968
- Determination of free amino groups in proteins by trinitrobenzenesulfonic acidAnalytical Biochemistry, 1966
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965