التفاصيل البيبلوغرافية
العنوان:
Catalytically Active Monomer of Glutathione S-Transferase π and Key Residues Involved in the Electrostatic Interaction between Subunits
المؤلفون:
Stephanie A. Misquitta , Elizabeth L. Adams , Roberta F. Colman , Sylvie Y. Blond , Yu-Chu Huang
المصدر:
Journal of Biological Chemistry . 283:32880-32888
بيانات النشر:
Elsevier BV, 2008.
سنة النشر:
2008
مصطلحات موضوعية:
Protein Conformation , Stereochemistry , Protein subunit , Molecular Sequence Data , Static Electricity , Molecular Conformation , Biochemistry , Catalysis , chemistry.chemical_compound , Protein structure , Humans , Amino Acid Sequence , Molecular Biology , Protein secondary structure , chemistry.chemical_classification , Sequence Homology, Amino Acid , Molecular mass , Circular Dichroism , Substrate (chemistry) , Cell Biology , Glutathione , Hydrogen-Ion Concentration , Protein Structure, Tertiary , Kinetics , Enzyme , Glutathione S-Transferase pi , chemistry , Protein Structure and Folding , Dimerization , Protein Binding
الوصف:
Human glutathione transferase pi (GST pi) has been crystallized as a homodimer, with a subunit molecular mass of approximately 23 kDa; however, in solution the average molecular mass depends on protein concentration, approaching that of monomer at
تدمد:
0021-9258
URL الوصول:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4588c254b6a530e6a5a76b57fab3b478 https://doi.org/10.1074/jbc.m805484200
حقوق:
OPEN
رقم الأكسشن:
edsair.doi.dedup.....4588c254b6a530e6a5a76b57fab3b478
قاعدة البيانات:
OpenAIRE
