The objective has been to establish if those ions which are known to change the stability of the struct,ure of proteins, have any influence on the properties of ionizable polypeptides. Potentiometric titrations and complementary optical rotation data are presented for aqueous solutions of poly-L-lys
Buoyant and potentiometric titrations of synthetic polypeptides III. Poly-l-lysine and poly-l-histidine in five salt solutions
β Scribed by James B. Ifft; Torben Graves Pedersen; Norman Fujita; Kathleen Kinzie
- Book ID
- 105651218
- Publisher
- Springer-Verlag
- Year
- 1978
- Weight
- 809 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0105-1938
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π SIMILAR VOLUMES
## Abstract The conformational changes of polyβ__N__^Ξ΅^βglutarylβLβlysine (PGL) and polyβ__N__^Ξ΅^βsuccinylβLβlysine (PSL) in various salt solutions were studied by use of ORD and potentiometric titration measurements. The addition of alkali metal salts to the fully ionized PGL or PSL solution cause
## Synopsis Aqiieoris solritions of poly-1,-tyrosine were studied by potentiometric titrations, lightsrat,teririg measrirements, and infrared spectroscopy in order to characterize the conformational changes the macromolecules exhibit when the hydrogen-ion concentration of the solutions is varied.