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Variants of beta2-microglobulin cleaved at lysine-58 retain the main conformational features of the native protein but are more conformationally heterogeneous and unstable at physiological temperature

DE LORENZI, ERSILIA;GIORGETTI, SOFIA
2006-01-01
2006
Biochemistry & Biophysics focuses on the structure and chemistry of biomolecules and covers all aspects of basic biochemistry/biophysics, including molecular structure, enzyme kinetics and protein-protein interaction; this category also contains cross-disciplinary resources focused on a specific class of biological molecules, e.g., nucleic acids, steroids, magnesium, growth factors, free radicals, bio-membranes, and peptides. Excluded are resources dealing with the application of biochemical techniques to specific topics listed elsewhere in CC/LS. Resources with a strong emphasis on the integration of biochemical pathways (such as signal transduction or molecular motors) at the cellular level are placed in the Cell & Developmental Biology category.
THE FEBS JOURNAL
000238389900011
2-s2.0-33646685225
Esperti anonimi
Inglese
Internazionale
STAMPA
273 (11)
2461
2474
14
Tematica Ex SIR: Studi di interazione fra farmaci e proteine amiloidogeniche (Classif. Ex SIR:Articoli su riviste ISI )
beta2-microglobulin; amyloidosis; protein conformation
11
info:eu-repo/semantics/article
262
Mimmi, M. C.; Jorgensen, T. J. D.; Pettirossi, F.; Corazza, A.; Viglino, P.; Esposito, G.; DE LORENZI, Ersilia; Pries, M.; Corlin, D. B.; Nissen, M. H...espandi
1 Contributo su Rivista::1.1 Articolo in rivista
none
1.1 Articolo in rivista
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11571/28113
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