Structural organization and stability of a thermoresistant domain generated by in vivo hydrolysis of the .alpha.-crystallin B chain from calf lens
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00153a022
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1. Post-translationally modified human lens crystallin fragments show aggregation in vitro;Biochemistry and Biophysics Reports;2017-07
2. Negative Charges in the C-terminal Domain Stabilize the αB-Crystallin Complex;Journal of Biological Chemistry;1998-10
3. Interaction of H+-ions with α-crystallin: solvent accessibility of ionizable side chains and surface charge;Biophysical Chemistry;1998-02
4. Molecular properties of glutamate dehydrogenase from the extreme thermophilic archaebacterium Sulfolobus solfataricus;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1995-09
5. Structure and Modifications of the Junior Chaperone alpha-Crystallin. From Lens Transparency to Molecular Pathology;European Journal of Biochemistry;1994-10
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