Primary sequence contribution to the optical function of the eye lens.

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Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins.Biophysical chemistry of the ageing eye lens.Crystal Structure of Chicken γS-Crystallin Reveals Lattice Contacts with Implications for Function in the Lens and the Evolution of the βγ-Crystallins.

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Primary sequence contribution to the optical function of the eye lens.

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http://www.wikidata.org/entity/Q40375255

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2014 nî lūn-bûn

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Primary sequence contribution to the optical function of the eye lens.

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Primary sequence contribution to the optical function of the eye lens.

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Primary sequence contribution to the optical function of the eye lens.

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Primary sequence contribution to the optical function of the eye lens

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B K Pierscionek

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C Elie

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K Mahendiran

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P2860

Gene ontology: tool for the unification of biology

The Protein Data Bank

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Crystal structure of truncated human betaB1-crystallin

PROMOTIF--a program to identify and analyze structural motifs in proteins

Biophysical Properties of γC-Crystallin in Human and Mouse Eye Lens: The Role of Molecular Dipoles

The betagamma-crystallin superfamily contains a universal motif for binding calcium

Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions

VMD: visual molecular dynamics

Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega

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srep05195

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10.1038/SREP05195

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English

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Jean-Christophe Nebel

Ali J Ryan

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Primary sequence contribution to the optical function of the eye lens.

about

P2860

P2860

Primary sequence contribution to the optical function of the eye lens.

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