title: About the albumin structure in solution: cigar Expanded form versus heart Normal shape.
abstract: 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.
authors.affiliation: Dipartimento di Chimica, Sapienza Università di Roma, P. le A. Moro 5, 00185 Roma, Italy. leggio@caspur.it
authors.forename: Claudia
authors.initials: C
authors.lastname: Leggio
authors.forename: Luciano
authors.initials: L
authors.lastname: Galantini
authors.forename: Nicolae Viorel
authors.initials: NV
authors.lastname: Pavel
mesh_terms: D000595:Amino Acid Sequence; D003198:Computer Simulation; D006801:Humans; D008027:Light; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012542:Scattering, Radiation; D053838:Scattering, Small Angle; D012709:Serum Albumin / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D012709:Serum Albumin