منابع مشابه
Genetically engineered immunoglobulins reveal structural features controlling segmental flexibility.
We have carried out nanosecond fluorescence polarization studies of genetically engineered immunoglobulins to determine the structural features controlling their segmental flexibility. The proteins studied were hybrids of a relatively rigid isotype (mouse IgG1) and a relatively flexible one (mouse IgG2a). They have identical light chains and heavy chain variable regions and have the same combin...
متن کاملInfluence of the hinge region on complement activation, C1q binding, and segmental flexibility in chimeric human immunoglobulins.
We have characterized a series of genetically engineered chimeric human IgG3 and IgG4 anti-dansyl (DNS) antibodies with identical antibody-combining sites but different hinge region amino acid compositions to determine how the hinge region influences Fab fragment segmental flexibility, C1q binding, and complement activation. Our data support the correlation between "upper hinge" length and Fab ...
متن کاملIn vitro analysis of the segmental flexibility of the thoracic spine
Basic knowledge about the thoracic spinal flexibility is limited and to the authors' knowledge, no in vitro studies have examined the flexibility of every thoracic spinal segment under standardized experimental conditions using pure moments. In our in vitro study, 68 human thoracic functional spinal units including the costovertebral joints (at least n = 6 functional spinal units per segment fr...
متن کاملFluorescence studies of chicken liver fatty acid synthase. Segmental flexibility and distance measurements.
The 4'-phosphopantetheine of chicken liver fatty acid synthase was specifically labeled with the fluorescent substrate analog coenzyme A 6-[7-nitrobenz-2-oxa-1,3-diazol-4-yl]aminohexanoate at low salt concentrations. A serine at the active site of the thioesterase was specifically labeled with the fluorescent compounds 6-[7-nitrobenz-2-oxa-1,3-diazol-4-yl]aminopentylmethylphosphono fluoridate a...
متن کاملSegmental flexibility in Escherichia coli ribosomal protein S1 as studied by fluorescence polarization.
Ribosomal protein S1 covalently reacts with approximately one equivalent of iodoacetylethylenediamine (1,5-napthol sulfonate (IAEDANS) or iodoacetylaminofluorescein (IAAF). The product AEDANS-S1 can bind to 30S ribosomal subunits lacking S1 as shown by polyacrylamide-agarose gel electrophoresis AEDANS-S1 and AAF-S1 when added back to S1-depleted 30S subunits modulate poly(U)-dependent polypheny...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1980
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(80)85003-x