Titlebook: Spectroscopy of Biological Molecules: New Directions; 8th European Confere J. Greve,G. J. Puppels,C. Otto Book 1999 Springer Science+Busine

A精确的

Nanosecond UV resonance Raman examination of initial steps in α-helix secondary structure evolutioncomplex energy landscapes, which efficiently funnel the folding towards the native form(s) [1–4]. It is essential to develop methods to predict the structure of functioning and mutated proteins from their primary sequences in order to devise strategies for alleviating human disease. We report here t

MURAL

fidelity

Orgasm

Characterization of the binding of endogenous proteins to endotoxins: binding stochiometry and prote the bacterial cells, a variety of biological effects in mammals. Various abundant endogenous LPS-binding proteins may, however, modify the response to LPS. Therefore, for an understanding of the interaction processes the characterisation of endotoxin binding to the proteins is of importance. For an

Malaise

Alteration of the internal dynamics of , alkaline phosphatase under proteolytic modification, thermaerature phosphorescence properties of Trp residues have been shown to be a sensitive monitor of the internal dynamics of the surrounding protein matrix [3–7]. In this work we take advantage of the exclusive sensitivity of the room temperature tryptophan phosphorescence (RTTP) lifetime to the local f

defendant

果核

圆锥体

渐强

泥土谦卑

Film formation from wheat gluten proteins by FTIR spectroscopyr, little information is available concerning protein network formation and polypeptide interactions in the film. The aim of this study was then to obtain basic informations about the modification of protein structures induced by film-forming processes.