• 한국정밀공학회:학술대회논문집
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• 한국정밀공학회 2008년도 춘계학술대회 논문집
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• pp.117-118
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• 2008

• 대한수학회보
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• 제33권2호
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• pp.277-287
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• 1996

The theory of integration of functions with values in a Banach space has long been a fruitful area of study. In the eight years from 1933 to 1940, seminal papers in this area were written by Bochner, Gelfand, Pettis, Birhoff and Phillips. Out of this flourish of activity, two integrals have proved to be of lasting: the Bochner integral of strongly measurable function. Through the forty years since 1940, the Bochner integral has a thriving prosperous history. But unfortunately nearly forty years had passed until 1976 without a significant improvement after B. J. Pettis's original paper in 1938 [cf. 11].

• Bulletin of the Korean Chemical Society
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• 제33권8호
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• pp.2508-2512
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• 2012

Cold shock proteins (CSPs) are a family of proteins induced at low temperatures. CSPs bind to single-stranded nucleic acids through the ribonucleoprotein 1 and 2 (RNP 1 and 2) binding motifs. CSPs play an essential role in cold adaptation by regulating transcription and translation via molecular chaperones. The solution nuclear magnetic resonance (NMR) or X-ray crystal structures of several CSPs from various microorganisms have been determined, but structural characteristics of psychrophilic CSPs have not been studied. Therefore, we optimized the purification process to obtain highly pure Lm-Csp and determined the three-dimensional structure model of Lm-Csp by comparative homology modeling using MODELLER on the basis of the solution NMR structure of Bs-CspB. Lm-Csp consists of a ${\beta}$-barrel structure, which includes antiparallel ${\beta}$ strands (G4-N10, F15-I18, V26-H29, A46-D50, and P58-Q64). The template protein, Bs-CspB, shares a similar ${\beta}$ sheet structure and an identical chain fold to Lm-Csp. However, the sheets in Lm-Csp were much shorter than those of Bs-CspB. The Lm-Csp side chains, E2 and R20 form a salt bridge, thus, stabilizing the Lm-Csp structure. To evaluate the contribution of this ionic interaction as well as that of the hydrophobic patch on protein stability, we investigated the secondary structures of wild type and mutant protein (W8, F15, and R20) of Lm-Csp using circular dichroism (CD) spectroscopy. The results showed that solvent-exposed aromatic side chains as well as residues participating in ionic interactions are very important for structural stability. Further studies on the three-dimensional structure and dynamics of Lm-Csp using NMR spectroscopy are required.