Application of Pulse Radiolysis to Biological Macromolecules
نویسندگان
چکیده
منابع مشابه
Some biological interactions studied by pulse radiolysis techniques.
Complex formation betwel'n proteins and ùrug ' , mLLco-poly,;accharide;, an1l dyes, or detergent typc molecules is well documentcd in tbc litcraturc ( 1•3) and has been studied b y a varicty of methods including ultrafiltration , dialysis and metachromatic spcctrometry. In this romrnunication we attempt to show that thesl' binding procc ses can be gcnerally investigated by pulsc radiolysis whic...
متن کاملIsir Subpicosecond Pulse Radiolysis System
The highest time resolution of the pulse radiolysis had remained about 30 ps since the late 1960’s. To make clear the primary processes in the radiation chemistry and physics within 30 ps, we developed a stroboscopic pulse radiolysis system for the absorption spectroscopy with the time resolution of 2.0 ps (10-90% rise time). The time resolution of 2.0 ps was estimated from the time-dependent b...
متن کاملPulse radiolysis of aqueous thiocyanate solution.
The pulse radiolysis of N(2)O saturated aqueous solutions of KSCN was studied under neutral pH conditions. The observed optical absorption spectrum of the SCN(*) radical in solution is more complex than previously reported, but it is in good agreement with that measured in the gas phase. Kinetic traces at 330 and 472 nm corresponding to SCN(*) and (SCN)(2)(*-), respectively, were fit using a Mo...
متن کاملCrystallography of Biological Macromolecules
Src homology 2 domain-containing protein tyrosine phosphatase [SHP] substrate 1 (SHPS-1), a receptor-type transmembrane glycoprotein whose cytoplasmic region binds and activates the protein tyrosine phosphatases SHP-1 and SHP-2, and thereby modulates multiple cellular functions. Its extracellular region regulates intercellular communication in the neural and immune systems through its associati...
متن کاملCrystallography of Biological Macromolecules
C218 located at the interface between A-band and M-line. It has been shown by Centner et al. [2] that MURF-1, a member of the RING finger proteins, binds to the two Ig-domains A168 and A169 in proximity to the kinase. Thus, its binding might be involved in the regulation of titin kinase. The structure of this tandem Ig domain has been solved. Ig domains, also in titin, are involved in many prot...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 1974
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.14.56