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Structural properties of polydisperse biopolymer solutions: A light scattering study of bovine α‐crystallin
Author(s) -
Schurtenberger P.,
Augusteyn R. C.
Publication year - 1991
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360311011
Subject(s) - chemistry , biopolymer , size exclusion chromatography , monomer , polymer , dynamic light scattering , protein quaternary structure , light scattering , molar mass distribution , polymerization , crystallography , static light scattering , bovine serum albumin , monotonic function , degree of polymerization , scattering , analytical chemistry (journal) , chemical engineering , chromatography , optics , organic chemistry , physics , biochemistry , protein subunit , nanoparticle , engineering , gene , enzyme , mathematical analysis , mathematics
We have measured 〈 R H 〉 z , 〈 R G 2 〉 Z ½, and 〈 M 〉 w for individual fractions of the protein α‐crystallin obtained by gel filtration of bovine lens nuclear extracts. A strong and monotonic decrease of 〈 R H 〉 z and 〈 M 〉 w with increasing elution volume could be observed, indicating a broad size distribution. The experimental results are quantitatively consistent with a polymerization of monomeric units into linear chains, which may have a certain degree of flexibility. Using theoretical expressions for 〈 R G 2 〉 and R H originally derived for semiflexible polymers in solution, we can self‐consistently analyse the data from static and dynamic light scattering, and from electron microscopy experiments. We thus obtain detailed information on the molecular weight distribution and the quaternary structure of α‐crystallin in these solutions.