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Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor

Journal Article · · Biophys. J.; (United States)
;
The exchange kinetics of the slowest exchanging BPTI ..beta..-sheet protons are complex compared to model peptides; the activation energy, E/sub a/, and the pH dependence are temperature dependent. We have measured the exchange kinetics in the range pH 1 to 11, 33 to 71/sup 0/C, particularly the temperature dependence. The data are fit to a model in which exchange of each proton is determined by two discrete dynamical processes, one with E/sub a/ approx. 65 kcal/mol and less than first order dependence on catalyst ion, and one with E/sub a/ 20 to 30 kcal/mol and approaching first order in catalyst ion. The low activation energy process is the mechanism of interest in the native conformation of globular proteins and involves low energy, small amplitude fluctuations; the high activation energy process involves major unfolding. The model is simple, has a precedent in the hydrogen exchange literature, and explains quantitatively the complex feature of the exchange kinetics of single protons in BPTI.
Research Organization:
Univ. of Minnesota, St. Paul
OSTI ID:
6795826
Journal Information:
Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 32:1; ISSN BIOJA
Country of Publication:
United States
Language:
English

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Related Subjects

550200* -- Biochemistry
551000 -- Physiological Systems
59 BASIC BIOLOGICAL SCIENCES
ACTIVATION ENERGY
ANIMALS
BARYONS
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL MODELS
BODY
CATTLE
CHARGE EXCHANGE
DIGESTIVE SYSTEM
DOMESTIC ANIMALS
DYNAMIC FUNCTION STUDIES
ELEMENTARY PARTICLES
ENDOCRINE GLANDS
ENERGY
ENZYME ACTIVITY
ENZYME INHIBITORS
ENZYMES
FERMIONS
GLANDS
HADRONS
HYDROLASES
KINETICS
MAMMALS
MOLECULAR STRUCTURE
NUCLEONS
ORGANS
PANCREAS
PEPTIDE HYDROLASES
PH VALUE
PROTONS
REACTION KINETICS
RESPONSE MODIFYING FACTORS
RUMINANTS
SERINE PROTEINASES
TEMPERATURE DEPENDENCE
TRYPSIN
VERTEBRATES