Length dependent folding kinetics of phenylacetylene oligomers: Structural characterization of a kinetic trap

2005 ◽  
Vol 122 (12) ◽  
pp. 124908 ◽  
Author(s):  
Sidney P. Elmer ◽  
Vijay S. Pande
Keyword(s):  
Structural Characterization ◽  
Folding Kinetics ◽  
Kinetic Trap ◽  
Kinetics Of

Experimental Characterization of the Folding Kinetics of the Notch Ankyrin Domain

2005 ◽  
Vol 352 (2) ◽  
pp. 266-281 ◽  
Author(s):  
Cecilia C. Mello ◽  
Christina Marchetti Bradley ◽  
Katherine W. Tripp ◽  
Doug Barrick
Keyword(s):  
Experimental Characterization ◽  
Folding Kinetics ◽  
Kinetics Of

Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering

1998 ◽  
Vol 276 (1) ◽  
pp. 225-237 ◽  
Author(s):  
Lingling Chen ◽  
Gudrun Wildegger ◽  
Thomas Kiefhaber ◽  
Keith O Hodgson ◽  
Sebastian Doniach
Keyword(s):  
Structural Characterization ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Lysozyme Refolding ◽  
Kinetics Of ◽  
Ray Scattering

scholarly journals Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience

2017 ◽  
Vol 13 ◽  
pp. 1145-1167 ◽  
Author(s):  
Serge Pérez ◽  
Daniele de Sanctis
Keyword(s):  
Synchrotron Radiation ◽  
Structural Characterization ◽  
Crystalline State ◽  
Structural Diversity ◽  
Interacting Proteins ◽  
X Ray ◽  
Wide Range ◽  
Kinetics Of

Synchrotron radiation is the most versatile way to explore biological materials in different states: monocrystalline, polycrystalline, solution, colloids and multiscale architectures. Steady improvements in instrumentation have made synchrotrons the most flexible intense X-ray source. The wide range of applications of synchrotron radiation is commensurate with the structural diversity and complexity of the molecules and macromolecules that form the collection of substrates investigated by glycoscience. The present review illustrates how synchrotron-based experiments have contributed to our understanding in the field of structural glycobiology. Structural characterization of protein–carbohydrate interactions of the families of most glycan-interacting proteins (including glycosyl transferases and hydrolases, lectins, antibodies and GAG-binding proteins) are presented. Examples concerned with glycolipids and colloids are also covered as well as some dealing with the structures and multiscale architectures of polysaccharides. Insights into the kinetics of catalytic events observed in the crystalline state are also presented as well as some aspects of structure determination of protein in solution.

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