A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution
A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution(414 views) Vergara A, Grassi M, Sica F, Pizzo E, D’Alessio G, Mazzarella L, Merlino A
Keywords: Atomic Resolution, Calcium Binding, Crystallins, Domain Interactions, Folding, Greek-Key Motif, Trp Corner, Tyr Corner, Animal, Article, Binding Site, Chemical Structure, Chemistry, Genetics, Geodia, Metabolism, Molecular Evolution, Protein Folding, Protein Motif, X Ray Crystallography, Amino Acid Motifs, X-Ray, Models, Geodia Cydonium, Metazoa, Vertebrata,
Affiliations: *** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, I-80126 Napoli, Italy
Istituto di Biostrutture e Bioimmagini (CNR), Via Mezzocannone 16, Napoli, Italy
Dipartimento di Biologia, Università Degli Studi di Napoli Federico II, Via Cintia, Napoli, Italy
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A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution
A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution
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A Novel Interdomain Interface In Crystallins: Structural Characterization Of The Beta Gamma-Crystallin From Geodia Cydonium At 0. 99 Angstrom Resolution