Physicochemical and structural characterization of iron–sucrose formulations: a comparative study

2013 ◽  
Vol 19 (5) ◽  
pp. 513-520 ◽  
Author(s):  
Bhavesh S. Barot ◽  
Punit B. Parejiya ◽  
Dharmik M. Mehta ◽  
Pragna K. Shelat ◽  
Gaurang B. Shah
Keyword(s):  
Comparative Study ◽  
Structural Characterization ◽  
Iron Sucrose

scholarly journals Kinetic and structural characterization of the self-labeling protein tags HaloTag7, SNAP-tag and CLIP-tag

2021 ◽  
Author(s):  
Jonas Wilhelm ◽  
Stefanie Kuehn ◽  
Miroslaw Tarnawski ◽  
Guillaume Gotthard ◽  
Jana Tuennermann ◽  
...  
Keyword(s):  
Comparative Study ◽  
Structural Characterization ◽  
Fusion Proteins ◽  
The Self ◽  
Substrate Specificities ◽  
Substrate Preferences ◽  
Diffusion Limited ◽  
Protein Tags ◽  
Selection Of

The self-labeling protein tags (SLPs) HaloTag7, SNAP-tag and CLIP-tag allow the covalent label-ing of fusion proteins with synthetic molecules for applications in bioimaging and biotechnology. To guide the selection of an SLP-substrate pair and provide guidelines for the design of sub-strates, we report a systematic and comparative study on the labeling kinetics and substrate specificities of HaloTag7, SNAP-tag and CLIP-tag. HaloTag7 reaches almost diffusion-limited labeling rates with certain rhodamine substrates, which are more than two orders of magnitude higher than those of SNAP-tag for the corresponding substrates. SNAP-tag labeling rates how-ever are less affected by the structure of the label than those of HaloTag7, which vary over six orders of magnitude for commonly employed substrates. Solving the crystal structures of Halo-Tag7 and SNAP-tag labeled with fluorescent substrates allowed us to rationalize their substrate preferences. We also demonstrate how these insights can be exploited to design substrates with improved labeling kinetics.

New ultrastructural findings about Borrelia burgdorferi by cryofixation, negative staining, thin sectioning and scanning techniques

1990 ◽  
Vol 48 (3) ◽  
pp. 582-583
Author(s):  
S. F. Hayes ◽  
M. D. Corwin ◽  
T. G. Schwan ◽  
D. W. Dorward ◽  
W. Burgdorfer
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Structural Characterization ◽  
Negative Staining ◽  
Low Speed ◽  
Thin Sectioning ◽  
Ultrastructural Findings

Characterization of Borrelia burgdorferi strains by means of negative staining EM has become an integral part of many studies related to the biology of the Lyme disease organism. However, relying solely upon negative staining to compare new isolates with prototype B31 or other borreliae is often unsatisfactory. To obtain more satisfactory results, we have relied upon a correlative approach encompassing a variety EM techniques, i.e., scanning for topographical features and cryotomy, negative staining and thin sectioning to provide a more complete structural characterization of B. burgdorferi.For characterization, isolates of B. burgdorferi were cultured in BSK II media from which they were removed by low speed centrifugation. The sedimented borrelia were carefully resuspended in stabilizing buffer so as to preserve their features for scanning and negative staining. Alternatively, others were prepared for conventional thin sectioning and for cryotomy using modified procedures. For thin sectioning, the fixative described by Ito, et al.

Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90

2011 ◽  
Vol 44 (06) ◽  
Author(s):  
A Bracher ◽  
C Kozany ◽  
AK Thost ◽  
F Hausch
Keyword(s):  
Structural Characterization ◽  
Ppiase Domain
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