Radiation stability of albumin preparations

Kuptsov, A. Kh.; L'vova, G. V.; Соболева, Н. Н.; Trofimov, V. I.; Chkheidze, I.I.

doi:10.1007/bf00767107

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1992

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“…13 One possible route to identification would be through isotopic substitution. For example, we find that for Cf = Cg = 13C the u ( C S ) for r#~,,\c/~ = c #~~, \ c /~ = P shift by 3-6 cm-' for x' = C (depending on x2), by [8][9][10][11] cm-' for X' = H, and by 11-16 cm-' for X' = N. Strong inferences about structure will require such approaches, but these are made possible by the more reliable insights provided by normal mode analysis.…”

Section: Discussionmentioning

confidence: 99%

Vibrational studies of the disulfide group in proteins. VI. General correlations of SS and CS stretch frequencies with disulfide bridge geometry

Qian

Krimm

1992

Biopolymers

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Normal mode calculations have been done on a range of disulfide bridge conformations in order to determine how the SS stretch and CS stretch frequencies depend on structure. In addition to varying the C alpha C beta SS and NC alpha C beta S dihedral angles, we have varied the phi, psi of the adjoining peptide groups since we have shown that these also influence the above frequencies. In order to obtain structural information from the observed frequencies, we have done a study of the conformational states found in 92 disulfide bridges in 25 known protein structures. This permits making a statistically based correlation between CS stretch frequencies and the possible contributing conformers.

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