Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 10, Issue 45, Pages 6741-6750Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/b808938h
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Funding
- MIUR [2006 039789-001]
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A structural comparison between the Normal and the Expanded isomers of the human serum albumin has been carried out by using small angle X-ray scattering (SAXS) and light scattering (LS) techniques. Geometrical bodies, recovered structures (GA_STRUCT code) and rigid body modeling (CRYSOL and BUNCH software) were used to obtain low-resolution 3D structures from one-dimensional scattering patterns. These restored shapes were also exploited to perform a correlation between SAXS and LS data. By attempting a detailed description of globular and unfolded protein structures in solution, we tried to propose a suitable approach to follow the path of folding/unfolding processes and to isolate and characterize possible partially folded intermediate states.
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