PROTEIN IONIZABLE GROUPS: pK VALUES AND THEIR CONTRIBUTION TO PROTEIN STABILITY AND SOLUBILITY C
نویسندگان
چکیده
PROTEIN IONIZABLE GROUPS: pK VALUES AND THEIR CONTRIBUTION TO PROTEIN STABILITY AND SOLUBILITY C. Nick Pace, Gerald R. Grimsley, and J. Martin Scholtz From the Department of Molecular and Cellular Medicine, Texas A&M Health Science Center, College Station, TX 77843 Running head: Protein pK values Address correspondence to: C. Nick Pace, Department of Molecular and Cellular Medicine, 440 Reynolds Medical Building, College Station, TX 77843-1114. Phone: 979-845-1788. FAX: 979-8479481. E-mail: [email protected]
منابع مشابه
Protein ionizable groups: pK values and their contribution to protein stability and solubility.
The structure, stability, solubility, and function of proteins depend on their net charge and on the ionization state of the individual residues. Consequently, biochemists are interested in the pK values of the ionizable groups in proteins and how these pK values depend on their environment. We review what has been learned about pK values of ionizable groups in proteins from experimental studie...
متن کاملEmulsifying Properties of Corn
Cereal Chem. 66(4):263-267 Emulsifying capacity and emulsion stability of hexane-defatted corn content; 70.39% water was retained by the emulsion. High emulsion germ protein obtained by modified and conventional extraction processes stability was obtained as the result of specific protein properties. Increasing were studied. Defatted corn germ protein obtained by the modified fat content in emu...
متن کاملImprovement of solubility and stability of the antimicrobial peptide nisin by protein engineering.
Nisin is a 3.4-kDa antimicrobial peptide that, as a result of posttranslational modifications, contains unsaturated amino acids and lanthionine residues. It is applied as a preservative in various food products. The solubility and stability of nisin and nisin mutants have been studied. It is demonstrated that nisin mutants can be produced with improved functional properties. The solubility of n...
متن کاملSequence-based prediction of protein solubility.
In order to investigate the relationship between the thermodynamics and kinetics of protein aggregation, we compared the solubility of proteins with their aggregation rates. We found a significant correlation between these two quantities by considering a database of protein solubility values measured using an in vitro reconstituted translation system containing about 70% of Escherichia coli pro...
متن کاملSystematic study of the physicochemical properties of a homologous series of aminobisphosphonates.
Aminobisphosphonates, e.g., alendronate and neridronate, are a well known class of molecules used as drugs for various bone diseases. Although these molecules have been available for decades, a detailed understanding of their most important physicochemical properties under comparable conditions is lacking. In this study, ten aminobisphosphonates, H(2)N(CH2)(n)C(OH)[P(O)(OH)(2)](2) in which n = ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2009