The conformation of proteins in chromatin. A circular dichroism study below 250 nm.
This paper is an investigation of the circular dichroism (CD) spectra of DNA and protein in chromatin. The circular dichroism (CD) of chromatin below 250 nm is due to DNA and protein peptide chromophores. The spectrum in this region is resolved into contributions from salt-extractable proteins (histone and non-histone proteins extractable with sodium chloride), residual non-histone proteins (not extractable with 3 M sodium chloride), and DNA. Below 250 nm, DNA in chromatin has the same CD spectrum as DNA free in solution, in contrast to the CD of DNA above 250 nm (Hjelm, R. and Huang, R. C., (1974), Biochemistry 13, 5275). Histones and salt-extractable non-histone proteins in chromatin are seen to have an average CD like those observed for globular proteins. The average CD of the residual non-histone proteins is consistent with a population of proteins with more extended conformation. The CD of each of these components is found to be the same in chromatins isolated from tissues having different nuclear synthetic activities: chick embryo brain, pig cerebellum, myeloma K41, calf thymus, and chicken erythrocyte.
D000818:Animals; D001923:Brain Chemistry; D002467:Cell Nucleus / Q000032:analysis; D002531:Cerebellum / Q000032:analysis; D002642:Chick Embryo; D002645:Chickens; D002843:Chromatin; D002942:Circular Dichroism; D004247:DNA / Q000097:blood; D004273:DNA, Neoplasm; D004912:Erythrocytes / Q000032:analysis; D006657:Histones; D007700:Kinetics; D008433:Mathematics; D009194:Myeloma Proteins / Q000032:analysis; D009690:Nucleic Acid Conformation; D009698:Nucleoproteins / Q000097:blood; D011485:Protein Binding; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013552:Swine
D002843:Chromatin; D004273:DNA, Neoplasm; D006657:Histones; D009194:Myeloma Proteins; D009698:Nucleoproteins; D004247:DNA