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Vibrational spectroscopy of the single Trp residue in hen egg-white lysozyme at pH 3.0: theoretical spectroscopy of tryptophan chi((2),(3),(2),(1)) and chi((3),(2),(1)) and identification of an experimental resonance in the low-frequency region.
The amide I’ and amide III’ band assignments of the single Trp residue in the hen egg-white lysozyme at pH 3.0 are investigated using high-resolution time-resolved resonance Raman spectroscopy. Their analyses suggest that the Trp-84 ring is in the equilibrium between the all-trans and the syn-gauche conformation, the C-S-C backbone torsion angle in the ground state around Trp-84 is about 45 degrees, and the average pucker of Trp-84 is C(2′) (gauche). The chi((3))s of Trp-84 is zero, which is an unusual case among Trp residues. The low-frequency components of the Trp-84 resonance Raman bands (0-900 cm(-)(1)) can be assigned to Trp-84, Val-83, Trp-97 and His-33, which are most likely involved in the main chain of the Trp-84 ring. The lowest-frequency peaks arise from the out-of-plane bending of the indole N-H bond, which is due to the coordinated dioxygen molecule (2250-2350 cm(-)(1)). The chi((2),(3),(2),(1)) and chi((3),(2),(1)) components of the Trp-84 resonance Raman bands are zero, which reveals that Trp-84 is the only Trp residue in the lysozyme molecule at pH 3.0.

The Great Book Designer Swindle [pdf] – gerbilly

======
bstar77
This is a very interesting read. The part where he explains the problem with
adding layering is a surprisingly underplayed side effect and I’m interested
in hearing more, especially if they accomplished this in a way that didn’t
pose a serious performance hit.

2013.8.2316 条件付
3e33713323

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