The thermal effect of the formation of the "burst-phase" folding intermediate has been studied using a titration calorimeter. It is shown that, unlike the total thermal effect of native structure formation, it can be both positive and negative depending on the temperature. The reasons for this paradoxical behavior are analyzed. A conclusion is drawn about the leading role of dehydration of non-polar groups in the first stage of folding.
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Inside of the burst-phase intermediate of a protein folding. Hydration of hydrophobic groups.
Biophys Chem
September 2024
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia. Electronic address:
The thermal effect of the formation of the "burst-phase" folding intermediate has been studied using a titration calorimeter. It is shown that, unlike the total thermal effect of native structure formation, it can be both positive and negative depending on the temperature. The reasons for this paradoxical behavior are analyzed.
View Article and Find Full Text PDFIonic conditions modulate stimulus-induced capacitance changes in isolated neurohypophysial terminals of the rat.
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January 2010
Physiology Department & Program in Neuroscience, University of Massachusetts, Medical School, Worcester, MA 01655, USA.
Peptidergic nerve terminals of the neurohypophysis (NH) secrete both oxytocin and vasopressin upon stimulation with peptide-specific bursts of action potentials from magnocellular neurons. These bursts vary in both frequency and action potential duration and also induce in situ ionic changes both inside and outside the terminals in the NH. These temporary effects include the increase of external potassium and decrease of external calcium, as well as the increase in internal sodium and chloride concentrations.
View Article and Find Full Text PDFProbing the interactions between the folding elements early in the folding of Escherichia coli dihydrofolate reductase by systematic sequence perturbation analysis.
J Mol Biol
March 2005
Protein Design Research Group, Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.
One of the necessary conditions for a protein to be foldable is the presence of a complete set of folding elements (FEs) that are short contiguous peptide segments distributed over an amino acid sequence. Previous studies indicated the FE assembly model of protein folding, in which the FEs interact with each other and coalesce to form an intermediate(s) early in the folding reaction. This suggests that a clue to the understanding of the determinants of protein foldability can be found by investigating how the FEs interact with each other early in the folding and thereby elucidating roles of the FEs in protein folding.
View Article and Find Full Text PDFTesting the relationship between foldability and the early folding events of dihydrofolate reductase from Escherichia coli.
J Mol Biol
April 2003
Protein Design Research Group, Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Tsukuba Central 6, 1-1-1 Higashi, Tsukuba, Ibakari 305-8566, Japan.
A "folding element" is a contiguous peptide segment crucial for a protein to be foldable and is a new concept that could assist in our understanding of the protein-folding problem. It is known that the presence of the complete set of folding elements of dihydrofolate reductase (DHFR) from Escherichia coli is essential for the protein to be foldable. Since almost all of the amino acid residues known to be involved in the early folding events of DHFR are located within the folding elements, a close relationship between the folding elements and early folding events is hypothesized.
View Article and Find Full Text PDFSodium dependence of the Na(+)-H+ exchanger in the pre-steady state. Implications for the exchange mechanism.
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Laboratory of Cardiovascular Science, National Institute on Aging, National Institutes of Health, Baltimore, Maryland 21224.
The pre-steady state time course of amiloride-sensitive Na+o uptake by the Na(+)-H+ exchanger in renal brush border membrane vesicles (BBMV) exhibits a burst phase at 0 degrees C which corresponds to the initial turnover of the exchanger (Otsu, K., Kinsella, J. L.
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