| Autor: |
Loo JA; Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Company, Ann Arbor, Michigan 48105, USA. Joseph.Loo@wl.com, Holler TP, Foltin SK, McConnell P, Banotai CA, Horne NM, Mueller WT, Stevenson TI, Mack DP |
| Jazyk: |
angličtina |
| Zdroj: |
Proteins [Proteins] 1998; Vol. Suppl 2, pp. 28-37. |
| DOI: |
10.1002/(sici)1097-0134(1998)33:2+<28::aid-prot5>3.3.co;2-p |
| Abstrakt: |
Mass spectrometry (MS) with electrospray ionization (ESI) has shown utility for studying noncovalent protein complexes, as it offers advantages in sensitivity, speed, and mass accuracy. The stoichiometry of the binding partners can be easily deduced from the molecular weight measurement. In many examples of protein complexes, the gas phase-based measurement is consistent with the expected solution phase binding characteristics. This quality suggests the utility of ESI-MS for investigating solution phase molecular interactions. Complexes composed of proteins from the human immunodeficiency virus (HIV) have been studied using ESI-MS. Multiply charged protein dimers from HIV integrase catalytic core (F185K) and HIV protease have been observed. Furthermore, the ternary complex between HIV protease dimer and inhibitor pepstatin A was studied as a function of solution pH. Zinc binding to zinc finger-containing nucleocapsid protein (NCp7) and the NCp7-psi RNA 1:1 stoichiometry complex was also studied by ESI-MS. No protein-RNA complex was observed in the absence of zinc, consistent with the role of the zinc finger motifs for RNA binding. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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