作者: R. Santus
DOI: 10.1007/978-94-009-7052-6_22
关键词:
摘要: It is shown, using a few examples, that laser flash spectroscopy and pulse radiolysis are convenient methods for studying the structure dynamics of proteins their interactions with nucleic acids or polynucleotides. In case hemoproteins short duration makes it possible to follow conformational changes in time scale expanding from nanosecond second. Selective attack by negatively charged halide radicals formed upon aqueous solutions determine aminoacid residues involved active site protein interaction DNA.