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Article

Truncation of motifs III and IV in human lens betaA3-crystallin destabilizes the structure.

Biochemistry - 22 Aug 2006

Gupta R, Srivastava K, Srivastava O P

Abstract excerpt

The purpose of our study was to determine the effects of specific truncations on the structural properties of human betaA3-crystallin. The following eight deletion mutants of betaA3-crystallin were generated: (i) N-terminal extension (NTE) 21 amino acids (betaA3[21] mutant), (ii) NTE 22 amino acids (betaA3[22] mutant), (iii) NTE (betaA3[N] mutant), (iv) NTE plus motif I (betaA3[N+I] mutant), (v) NTE plus motifs I...

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Share to Circular Dichroism
Share to Hydrophobic and Hydrophilic Interactions
Share to Lens, Crystalline

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Denaturation

Share to Scattering, Radiation

Share to Spectrometry, Fluorescence

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Source

Identifiers

PMID: 16906755
DOI: 10.1021/bi060499v

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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