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X-Ray diffraction studies of the conformation of macromolecules in solution. III. The helix–coil transition

✍ Scribed by George W. Brady; R. Salovey

Publisher
Wiley (John Wiley & Sons)
Year
1967
Tongue
English
Weight
344 KB
Volume
5
Category
Article
ISSN
0006-3525

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✦ Synopsis

Incorpoi.ated, dlurray Hill, Neic Jersey 07971

Synopsis

The procedure outlined in the previous paper of this series is applied t,o x-ray diffraction pat.t.erns of labeled polytyrosine in dimethylformamide-t,rifluoroacetic acid solutions. The a-helix appears to transform into the random coil conformation at a trifliioroacetic acid concent,rat.ion between 40 and 42.5%. Comparison of these results witsh those measured in t,he same system by optical rotation are in essential agreement.

📜 SIMILAR VOLUMES

Conformation of polypeptide in the, heli
Conformation of polypeptide in the, helix–coil transition region
✍ T. M. Birshtein 📂 Article 📅 1969 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 96 KB

## Conformation of Polypeptide i n the Helix-Coil Transition Region A recently published work by Go, Saito, and Ochiail presented a calculation of the mean values of the second (R2) and the fourth (R4) powers of the end-to-end distance of the polypeptide chain in the helix-coil transition region.

Studies of the helix–coil transition of
Studies of the helix–coil transition of poly-L-lysine in film and solution
✍ Hajime Noguchi 📂 Article 📅 1966 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 490 KB 👁 1 views

Water-insoluble films of poly-L-lysine, crosslinked with formaldehyde, were suspended in aqueous media and their relative lengths measured as a function of pH. A sharp transition of the polymer was observed in the pH range which corresponded with that observed in polylysine solutions by optical rota