Laser light-scattering evidence for an altered association of βB1-crystallin deamidated in the connecting peptide

Protein Science

Volumn 13, Issue 3, 2004, Pages 678-686

  Harms, Michael J ^a   Wilmarth, Philip A ^a   Kapfer, Deborah M ^a   Steel, Eric A ^b   David, Larry L ^a   Bächinger, Hans Peter ^b   Lampi, Kirsten J ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^b SHRINERS HOSPITAL FOR CHILDREN   (United States)

Author keywords

Cataracts; Deamidation; Laser light scattering; Lens crystallins; Mass spectrometry; Oligomer assembly

Indexed keywords

ASPARAGINE; BETA CRYSTALLIN; GLUTAMINE; OLIGOMER; PEPTIDE;

ADULT; ARTICLE; CATARACT; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); CRYSTAL STRUCTURE; DEAMINATION; HEAT; HUMAN; HUMAN TISSUE; LASER; LENS; LIGHT SCATTERING; MASS SPECTROMETRY; MUTANT; PRIORITY JOURNAL; PROTEIN ANALYSIS; VERTEBRATE; WILD TYPE;

AMIDES; ASPARAGINE; BETA-CRYSTALLIN B CHAIN; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CRYSTALLINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLUTAMINE; HEAT; HUMANS; LASERS; MASS SPECTROMETRY; MIDDLE AGED; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; NEPHELOMETRY AND TURBIDIMETRY; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; SCATTERING, RADIATION;

VERTEBRATA;

EID: 1342268073     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03427504     Document Type: Article

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