Protein Conformational Changes Determined by Matrix-Assisted Laser Desorption Mass Spectrometry

Conformational Stabilization of Rat S-Adenosylmethionine Decarboxylase by Putrescine

“…32) In order to examine the effect of putrescine on the susceptibility of AdoMetDC to trypsin, purified rat AdoMetDC was digested with trypsin in the presence or absence of putrescine and analyzed by MALDI-TOF MS at various time intervals (Fig. 4).…”

“…32) Putrescine-free AdoMetDC was digested with trypsin in the presence or absence of 0.3 mM putrescine in 0.05 M Tris-HCl buffer, pH 8.0, at 37°C. The molar ratio of AdoMetDC to trypsin was about 50 : 1.…”

“…30,31) In addition, susceptibility to proteolysis has been shown to be a sensitive method for detecting subtle conformation changes in proteins. 32,33) In this study, we examined the effect of putrescine on the conformation and activity of AdoMetDC purified from rat prostate using MALDI-TOF MS, and the susceptibility of AdoMetDC to trypsin following treatment with iodoacetic acid (IAA). We also examined the correlation between the presence of putrescine and stimulation of AdoMetDC activity and incorporation of IAA.…”

Perspectives on the chemical etiology of breast cancer.

“…Higher levels are found in grill scrapings, meat drippings, and pan residues (116). Some heterocyclic amines can be detected in the cooking fumes (117,118). In contrast, the cooking of meats by stewing, poaching, or microwaving does not lead to the formation of heterocyclic amines.…”

Distribution and Transition of Native and Completely Unfolded Conformations in the Unfolding of Bovine Heart Cytochrome c Induced by Urea and Guanidine Hydrochloride

“…Wherein, horse heart cytochrome c may be the most used cytochrome c molecules. For example, Harrington studied the unfolding of horse ferricytochrome c in the presence of several inorganic salts under a variety of denaturing conditions by means of viscosity measurements and absorbance changes in the Soret and visible regions; 5 Nieman et al studied the 13 C NMR spectroscopy of acetyltyrosyl-guanidinated horse heart cytochrome c; 6 Hagihara et al compared the stability of the native and acidic molten globule states of horse ferricytochrome c against heat, urea and guanidine hydrochloride using the intact species and species modified by various degrees of acetylation of the lysyl ε-amino groups; 7 Zhu et al investigated the conformational transition of horse heart cytochrome c induced by bromopyrogal red in very low concentration by dynamic spectro-electrochemical technique; 8 Zhang et al studied the denaturation of horse heart cytochrome c induced by bromopyrogal red by scanning tunnelling microscopy on the electrochemically pretreated highly oriented pyrolytic graphite surface; 9 Yang et al studied conformational changes of horse heart cytochrome c determined by matrix-assisted laser desorption mass spectrometry; 10 Moosavi-Movahedi et al studied the differential scanning calorimetry of the molten globule state of horse heart cytochrome c induced by sodium n-dodecyl sulfate; 11 Krylov et al studied the denaturation and renaturation of horse heart cytochrome c immobilized on gold electrodes in DMSO-containing buffers; 12 Kumar et al studied the alkali molten globule state of horse ferricytochrome c in "cold denaturation"; 13 Latypov et al studied the equilibrium and kinetic properties of reduced horse heart cytochrome c in the presence of carbon monoxide; 14 Baker and Heller studied the characteristics of equine heart cytochrome c in aqueous solutions of the fully water-miscible IL 1-butyl-3-methyl-imidazolium chloride by small-angle neutron and X-ray scattering; 15 Liu and Konermann characterized the solution-phase properties of horse heart cytochrome c after heat exposure by electrospray ionization mass spectrometry in conjunction with hydrogen/deuterium exchange and optical spectroscopy. 16 Like horse heart cytochrome c, cytochrome c from bovine heart is also a globular protein molecule.…”