✦ LIBER ✦

Ultraviolet resonance Raman spectra of hemoglobin excited at 200 and 218 nm: tertiary and quaternary structure differences

✍ Scribed by Copeland, Robert A.; Dasgupta, Siddharth; Spiro, Thomas G.

Book ID: 121336229
Publisher: American Chemical Society
Year: 1985
Tongue: English
Weight: 270 KB
Volume: 107
Category: Article
ISSN: 0002-7863
DOI: 10.1021/ja00297a065

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Ultraviolet resonance Raman spectra of i

Ultraviolet resonance Raman spectra of insulin and .alpha.-lactalbumin with 218 and 200-nm laser excitation

✍ Rava, Richard P.; Spiro, Thomas G. 📂 Article 📅 1985 🏛 American Chemical Society 🌐 English ⚖ 528 KB

Ultraviolet resonance Raman spectroscopy

Ultraviolet resonance Raman spectroscopy of hemoglobin with 200 and 212 nm excitation: H-bonds of tyrosines and prolines

✍ Xiaojie Zhao; Thomas G. Spiro 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 339 KB

Resonance Raman spectra are reported for hemoglobin (Hb) with deep UV excitation at 212 and 200 nm. At 200 nm, strongly enhanced amide bands appear, but the spectra are dominated by tyrosine residues, and substantial enhancement is seen for the Y7aº mode, a sensitive monitor of H-bond status. T-R di