Internal energy effects on the solvation and reactivity of multiply charged biomolecules for electrospray ionization mass spectroscopy. [Bovine ubiquitin]

Conference · Mon Jun 01 00:00:00 EDT 1992

OSTI ID:7107564

Light-Wahl, K J; Winger, B E; Rockwood, A L; Smith, R D

Mild (capillary) interface conditions which do not completely desolvate the ions of proteins in electrospray ionization mass spectrometry (ESI-MS) may be required to probe the higher order structures and weak associations. For the small protein bovine ubiquitin, two ion distributions (unsolvated ions and unresolved solvated ions) were observed. The resolvable solvation for leucine-enkephalin with methanol and water shows that the use of countercurrent N{sub 2} flow at the capillary affects the solvation observed. 2 figs. (DLC)

• Research Organization: Pacific Northwest Lab., Richland, WA (United States)
• Sponsoring Organization: USDOE; USDOE, Washington, DC (United States)
• DOE Contract Number: AC06-76RL01830
• OSTI ID: 7107564
• Report Number(s): PNL-SA-20444; CONF-9205196-5-Extd.Abst.; ON: DE92019140
• Resource Relation: Conference: 40. ASMS conference on mass spectrometry and allied topics, Washington, DC (United States), 31 May - 2 Jun 1992
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
ENKEPHALINS
STRUCTURAL CHEMICAL ANALYSIS
PROTEINS
CAPILLARIES
INTERFACES
LEUCINE
MASS SPECTROSCOPY
METHANOL
MOLECULAR STRUCTURE
SOLVATION
WATER
ALCOHOLS
AMINO ACIDS
AUTONOMIC NERVOUS SYSTEM AGENTS
BLOOD VESSELS
BODY
CARBOXYLIC ACIDS
CARDIOVASCULAR SYSTEM
DRUGS
ENDORPHINS
HYDROGEN COMPOUNDS
HYDROXY COMPOUNDS
NEUROREGULATORS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANS
OXYGEN COMPOUNDS
PEPTIDES
POLYPEPTIDES
SPECTROSCOPY
550200* - Biochemistry