Showing papers by "ICM Partners published in 1999"

Profiting from intellectual capital

Abstract: Intellectual capital (IC) is a significant resource for many companies This paper explains what IC is, the benefits IC can generate, how a firm can utilize those benefits, the different roles a portfolio of IC assets can play, how firms can extract value from these portfolios, and the risks to a company that does not manage its intellectual property portfolio The paper describes the steps for extracting value and outlines several ways to manage the firm’s IC assets It discusses how a firm determines the three major elements of context and different procedures firms may opt to follow internally to realize their intellectual value This paper also describes the ICM Gathering Group, the group of companies that have collectively created the knowledge the paper conveys The paper explains how the Gathering has defined intellectual capital and how its member companies use their knowledge to the benefit of their respective organizations

Equilibrium unfolding CD studies of bovine beta-lactoglobulin and its 14-52 fragment at acidic pH.

Abstract: Bovine β-lactoglobulin represents an interesting example of context-dependent secondary structure induction. In fact, secondary structure predictions indicated that this β-barrel protein has a surprisingly high α-helical preference, which was retained for short fragments. Cooperative transitions from the native β-sheet to α-helical structures were additionally induced by organic solvents, in particular trifluoroethanol. As a result of this high α-helical preference, it has been proposed that non-native α-helical intermediates could be formed in the unfolding pathway of this protein. In order to provide a better understanding of the processes that underlie conformational plasticity in this protein, CD measurements in the presence of increasing amounts of urea and in the presence of organic solvents were performed. Urea unfolding studies, performed at pH 2.1 and 37°C, revealed an apparent two-state transition, and afforded no evidence of non native α-helical intermediates. The protein treated with up to 6M urea, refolded to the native structure, while treatment with higher molar concentration urea, lead to partial misfolding. A 29-mer peptide covering the region of strands a and b of the intact protein, characterized by the presence of 4/3 heptad repeats, was synthesized and studied by CD in the presence of different solvents. On the basis of the obtained results, a mechanism was proposed to explain the structural transition from the β to α structure, provoked by organic solvents in the intact protein. © 1999 John Wiley & Sons, Inc. Biopoly 49: 441–450, 1999

On the application of statistical physics for the description of nonequilibrium effects in chemical systems

Abstract: In this paper we show how the methods of statistical physics may be applied to describe the nonequilibrium effects in systems with thermally activated reactions. A special attention is given to systems with multiple reactions, in which such effects are more important then in systems with a single reaction. Considering a model reaction scheme we demonstrate that a simple phenomenology, which associates different temperatures to different reagents, gives an accurate description of the nonequilibrium effects.