βB2 βB5

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a b c βB2 βB5 βD3 βD4 βD5 βD6 βF3 αB5 αB6 αB8 αB9

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c. a. b. βB2 βB5. βD3 βD4 βD5 βD6. βF3. αB5 αB6 αB8 αB9. - PowerPoint PPT Presentation

Transcript of βB2 βB5

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βB2 βB5 βD3 βD4 βD5 βD6 βF3 αB5 αB6 αB8 αB9

Formation and crystallization of the eye lens heterodimer βB2-βB3-crystallin

Formation and crystallization of the eye lens heterodimer βB2-βB3-crystallin

Eye lens βB2-crystallin: circular permutation does not influence the oligomerization state but enhances the conformational stability

Eye lens βB2-crystallin: circular permutation does not influence the oligomerization state but enhances the conformational stability

Calcium-binding to lens βB2- and βA3-crystallins suggests that all β-crystallins are calcium-binding proteins

Calcium-binding to lens βB2- and βA3-crystallins suggests that all β-crystallins are calcium-binding proteins

Loss of the C-terminal serine residue from bovine βB2-crystallin

Loss of the C-terminal serine residue from bovine βB2-crystallin

The importance of the last strand at the C-terminus in βB2-crystallin stability and assembly

The importance of the last strand at the C-terminus in βB2-crystallin stability and assembly

Regulatory Elements in the Rat βB2-crystallin Promoter

Regulatory Elements in the Rat βB2-crystallin Promoter

Solution conformation of bovine lens α-and βB2-crystallin terminal extensions

Solution conformation of bovine lens α-and βB2-crystallin terminal extensions

1H-NMR spectroscopy of bovine lens β-crystallin : The role of the βB2-crystallin C-terminal extension in aggregation

1H-NMR spectroscopy of bovine lens β-crystallin : The role of the βB2-crystallin C-terminal extension in aggregation

Cataract-linked mutation R188H promotes βB2-crystallin aggregation and fibrillization during acid denaturation

Cataract-linked mutation R188H promotes βB2-crystallin aggregation and fibrillization during acid denaturation

Amino acid sequence of human lens βB2-crystallin

Amino acid sequence of human lens βB2-crystallin

Mutation of interfaces in domain-swapped human βB2-crystallin

Mutation of interfaces in domain-swapped human βB2-crystallin

Formation of βA3/βB2-crystallin mixed complexes: involvement of N- and C-terminal extensions

Formation of βA3/βB2-crystallin mixed complexes: involvement of N- and C-terminal extensions

1H-NMR spectroscopy of βB2-crystallin from bovine eye lens : Conformation of the N- and C-terminal extensions

1H-NMR spectroscopy of βB2-crystallin from bovine eye lens : Conformation of the N- and C-terminal extensions

Folding and self-assembly of the domains of βB2-crystallin from rat eye lens

Folding and self-assembly of the domains of βB2-crystallin from rat eye lens

X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins

X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins

The N-terminal domain of βb2-crystallin resembles the putative ancestral homodimer

The N-terminal domain of βb2-crystallin resembles the putative ancestral homodimer

Structure of oligomeric βB2-crystallin: an application of the T2 translation function to an asymmetric unit containing two dimers

Structure of oligomeric βB2-crystallin: an application of the T2 translation function to an asymmetric unit containing two dimers

Sites of Glycation of βB2-Crystallin by Glucose and Fructose

Sites of Glycation of βB2-Crystallin by Glucose and Fructose

Nucleotide Sequence for the cDNA of the Bovine βB2 Crystallin and Assignment of the Orthologous Human Locus to Chromosome 22

Nucleotide Sequence for the cDNA of the Bovine βB2 Crystallin and Assignment of the Orthologous Human Locus to Chromosome 22

The Cooperation Between Two Silencers Creates an Enhancer Element that Controls Both the Lens-Preferred and the Differentiation Stage-Specific Expression of the Rat βB2-Crystallin Gene

The Cooperation Between Two Silencers Creates an Enhancer Element that Controls Both the Lens-Preferred and the Differentiation Stage-Specific Expression of the Rat βB2-Crystallin Gene