Biochemical and biophysical characterization of a plant calmodulin: Role of the N- and C-lobes in calcium binding, conformational change, and target interaction

2016 ◽  
Vol 1864 (3) ◽  
pp. 297-307 ◽  
Author(s):  
Alessandra Astegno ◽  
Valentina La Verde ◽  
Valerio Marino ◽  
Daniele Dell'Orco ◽  
Paola Dominici
Keyword(s):  
Conformational Change ◽  
Calcium Binding ◽  
Biophysical Characterization ◽  
Target Interaction

scholarly journals Dissecting the role of glutamine in seeding peptide aggregation

2020 ◽  
Author(s):  
Exequiel E. Barrera ◽  
Francesco Zonta ◽  
Sergio Pantano
Keyword(s):  
Molecular Weight ◽  
Structural Heterogeneity ◽  
Low Molecular Weight ◽  
Biophysical Characterization ◽  
Aggregation Propensity ◽  
Toxic Species ◽  
Dynamical Nature ◽  
Spatio Temporal

ABSTRACTPoly glutamine and glutamine-rich peptides play a central role in a plethora of pathological aggregation events. However, biophysical characterization of soluble oligomers —the most toxic species involved in these processes— remains elusive due to their structural heterogeneity and dynamical nature. Here, we exploit the high spatio-temporal resolution of simulations as a computational microscope to characterize the aggregation propensity and morphology of a series of polyglutamine and glutamine-rich peptides. Comparative analysis of ab-initio aggregation pinpointed a double role for glutamines. In the first phase, glutamines mediate seeding by pairing monomeric peptides, which serve as primers for higher-order nucleation. According to the glutamine content, these low molecular-weight oligomers may then proceed to create larger aggregates. Once within the aggregates, buried glutamines continue to play a role in their maturation by optimizing solvent-protected hydrogen bonds networks.TOC / Abstract Figure

scholarly journals Structural Characterization of the Conformational Change in Calbindin-D28kupon Calcium Binding Using Differential Surface Modification Analyzed by Mass Spectrometry

Biochemistry ◽  
2009 ◽  
Vol 48 (36) ◽  
pp. 8603-8614 ◽  
Author(s):  
Carey A. Hobbs ◽  
Leesa J. Deterding ◽  
Lalith Perera ◽  
Benjamin G. Bobay ◽  
Richele J. Thompson ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Surface Modification ◽  
Conformational Change ◽  
Structural Characterization ◽  
Calcium Binding

High-Resolution Measurements of Subsarcomere Calcium-Binding Distributions from EPXMA Images

1996 ◽  
Vol 54 ◽  
pp. 292-293
Author(s):  
M. E. Cantino ◽  
J. G. Eichen
Keyword(s):  
Calcium Binding ◽  
Thin Filament ◽  
Direct Evidence ◽  
Striated Muscle ◽  
Regulatory Protein ◽  
Psoas Muscle ◽  
Thin Filaments ◽  
Regulation Of Contraction

The distribution of calcium binding to thin filaments in vertebrate striated muscle provides clues about the role of calcium in regulation of contraction. A number of studies have suggested that the extent of Ca binding to the thin filament regulatory protein, troponin, is enhanced by the attachment of crossbridges. Electron probe X-ray microanalysis (EPXMA) has provided direct evidence of this enhancement by showing that more Ca is found in the overlap than in the nonoverlap region of sarcomeres in skinned rabbit psoas muscle in rigor. In that study, characterization of the spatial extent of this enhancement was limited by the pixel width of bands (4 pixels) within which Ca counts were averaged at each position across the sarcomere. In order to improve the resolution with which data are extracted from the image we have developed an automated routine for averaging calcium counts from successive columns of pixels across each half sarcomere in the image.

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