ISSN:
1432-1017
Schlagwort(e):
X-ray solution scattering
;
synchrotron radiation
;
chicken erythrocyte chromatin
;
rat liver chromatin
;
micrococcal nuclease
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Physik
Notizen:
Abstract Changes in the structure of chicken erythrocyte chromatin fibres at low ionic strength resulting from enzymatic digestion, thermal denaturation and binding of Netropsin and Distamycin were monitored by synchrotron X-ray solution scattering. Digestion with micrococcal nuclease confirms the previous assignment of the 0.05 nm-1 band to an interference between nucleosomes with an average distance of 23 nm. The results of thermal denaturation indicate that above 40°C there is a progressive increase of the internucleosomal distance and that above 60°C the characteristic structure of the chromatin fibre is destroyed. Binding of Netropsin and Distamycin also results in an increase of the internucleosomal distance which can be estimated to correspond to about 0.2 nm/mol.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00263677
