pH-Dependent Conformational Change of Fe3+-Binding Giant DNA for Control of Aggregation of Gold Nanoparticles

2011 ◽  
Vol 11 (6) ◽  
pp. 4724-4732
Author(s):  
Lingling Lin ◽  
Yan Zhang ◽  
Zengfang Feng ◽  
Na Li ◽  
Nannan Han ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Conformational Change ◽  
Ph Dependent

scholarly journals 3P037 pH-dependent conformational change of equine beta-lactoglobulin

2004 ◽  
Vol 44 (supplement) ◽  
pp. S199
Author(s):  
M. Ohkouchi ◽  
K. Nagashima ◽  
Y. Yamada ◽  
M. Ikeguchi
Keyword(s):  
Conformational Change ◽  
Ph Dependent ◽  
Beta Lactoglobulin

scholarly journals Comparing the folding landscapes of evolutionarily divergent procaspase-3

2022 ◽  
Author(s):  
Liqi Yao ◽  
Clay Clark
Keyword(s):  
Conformational Change ◽  
Common Ancestor ◽  
Folding Pathway ◽  
Free Energies ◽  
Folding Intermediates ◽  
Effector Caspases ◽  
The Common ◽  
Ph Dependent ◽  
Species Specific ◽  
Dimeric Intermediate

All caspases evolved from a common ancestor and subsequently developed into two general classes, inflammatory or apoptotic caspases. The caspase-hemoglobinase fold has been conserved throughout nearly one billion years of evolution and is utilized for both the monomeric and dimeric subfamilies of apoptotic caspases, called initiator and effector caspases, respectively. We compared the folding and assembly of procaspase-3b from zebrafish to that of human effector procaspases in order to examine the conservation of the folding landscape. Urea-induced equilibrium folding/unfolding of procaspase-3b showed a minimum three-state folding pathway, where the native dimer isomerizes to a partially folded dimeric intermediate, which then unfolds. A partially folded monomeric intermediate observed in the folding landscape of human procaspase-3 is not well-populated in zebrafish procaspase-3b. By comparing effector caspases from different species, we show that the effector procaspase dimer undergoes a pH-dependent conformational change, and that the conformational species in the folding landscape exhibit similar free energies. Together, the data show that the landscape for the caspase-hemoglobinase fold is conserved, yet it provides flexibility for species-specific stabilization or destabilization of folding intermediates resulting in changes in stability. The common pH-dependent conformational change in the native dimer, which yields an enzymatically inactive species, may provide an additional, albeit reversible, mechanism for controlling caspase activity in the cell.

scholarly journals A pH-dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system

FEBS Journal ◽  
2005 ◽  
Vol 272 (11) ◽  
pp. 2773-2783 ◽  
Author(s):  
Tomoaki Kato ◽  
Daizo Hamada ◽  
Takashi Fukui ◽  
Makoto Hayashi ◽  
Takeshi Honda ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Conformational Change ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Escherichia Coli O157 ◽  
Type Iii ◽  
Ph Dependent

pH-Dependent growth of atomic Pd layers on trisoctahedral gold nanoparticles to realize enhanced performance in electrocatalysis and chemical catalysis

Nanoscale ◽  
2018 ◽  
Vol 10 (47) ◽  
pp. 22302-22311 ◽  
Author(s):  
Yahui Song ◽  
Chensheng Xiang ◽  
Cuixia Bi ◽  
Chenshuo Wu ◽  
Hongpeng He ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Chemical Catalysis ◽  
Ph Dependent ◽  
Dependent Growth

Trisoctahedral gold nanoparticles with atomic Pd layers by the pH-dependent growth can be used in catalysis and in situ SERS monitoring.

A 360-MHz photo-CIDNP study of bovine pancreatic phospholipase A2. Observation of a pH-dependent conformational change

1979 ◽  
Vol 101 (24) ◽  
pp. 7397-7399 ◽  
Author(s):  
Eugene H. J. M. Jansen ◽  
Gustaaf J. M. Van Scharrenburg ◽  
Arend J. Slotboom ◽  
Gerard H. De Haas ◽  
Robert Kaptein
Keyword(s):  
Phospholipase A2 ◽  
Conformational Change ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2 ◽  
Ph Dependent
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