Allowance for effects of electrostatic repulsion on protein dimerization

Agapow P.-M. and Winzor D.J. (1988) Allowance for effects of electrostatic repulsion on protein dimerization. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 953 C: 197-200. doi:10.1016/0167-4838(88)90024-6


Author Agapow P.-M.
Winzor D.J.
Title Allowance for effects of electrostatic repulsion on protein dimerization
Journal name Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
ISSN 0167-4838
Publication date 1988
Sub-type Article (original research)
DOI 10.1016/0167-4838(88)90024-6
Volume 953
Issue C
Start page 197
End page 200
Total pages 4
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
1315 Structural Biology
2700 Medicine
Abstract A simple procedure for assessing the extent of electrostatic effects on protein dimerization is described and illustrated by application to published results on the ionic strength dependence of the dimerization constant for α-chymotrypsin at pH 4 (Aune, K.C., Goldsmith, L.C. and Timasheff, S.N. (1971) Biochemistry 10, 1617-1622). From the analysis it is concluded that the inverse dependence of α-chymotrypsin dimerization upon ionic strength is predominantly a general electrostatic effect, rather than a consequence of repulsion between two specific charged residues on the adjacent monomers comprising dimer.
Keyword Electrostatic effect
Protein dimerization
α-Chymotrypsin
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import
 
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