A quantitative model of cooperative effects in aspartate transcarbamylase and related hybrid molecules
- 1 January 1975
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 14 (1) , 19-32
- https://doi.org/10.1002/bip.1975.360140103
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- A general approach to co-operativity and its application to the oxygen equilibrium of hemoglobin and its effectorsJournal of Molecular Biology, 1974
- Interaction between polypeptide chains within the catalytic subunit of aspartate transcarbamylaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1973
- Structure and arrangement of the regulatory subunits in aspartate transcarbamylaseBiochemistry, 1972
- Time‐dependent model for hemoglobin and allosteric enzymes. I. General formulationBiopolymers, 1971
- Models for hemoglobin and allosteric enzymesBiopolymers, 1968
- Denaturation and renaturation of DNA. II. Possible use of synthetic periodic copolymers to establish model and parametersBiopolymers, 1968
- Denaturation and renaturation of DNA. I. Equilibrium statistics of copolymeric DNABiopolymers, 1966
- Comparison of Experimental Binding Data and Theoretical Models in Proteins Containing Subunits*Biochemistry, 1966
- On the nature of allosteric transitions: A plausible modelJournal of Molecular Biology, 1965
- On the Theory of the Ising Model of FerromagnetismReviews of Modern Physics, 1953