GrainGenes Reference Report: CCM-77-107
Reference
CCM-77-107
Title
Atomic force microscopy (AFM) study of interactions of HMW subunits of wheat glutenin
Journal
Cereal Chemistry
Year
2000
Volume
77
Pages
107-110
Author
Humphris ADL
[ Show all 6 ]
Abstract
Summary: Atomic force microscopy (AFM) has been used to study the non-covalent interactions of alkylated HMW subunit 1Dx5 and a M(r) 58,000 peptide derived from the central repetitive domain. Both protein and peptide align side-by-side to form fibrils, the HMW subunit forming a branched network, and the peptide forming linear rods. The N- and C-terminal domains of the subunit would, therefore, appear to contain regions that interact through noncovalent interactions in the absence of disulfide bond formation. These regions may be of importance in facilitating disulfide bond formation during protein body development
Keyword
domain glutenin m(r) m-r peptide
GrainGenes is a product of the Agricultural Research Service of the US Department of Agriculture.
GrainGenes Reference Report: CCM-77-107
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GrainGenes is a product of the Agricultural Research Service of the US Department of Agriculture. | |||