Liangcai Gu

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Small heat-shock proteins (sHsps) of various origins exist commonly as oligomers and exhibit chaperone-like activities in vitro. Hsp16.3, the sHsp from Mycobacterium tuberculosis, was previously shown to exist as a monodisperse nonamer in solution when analyzed by size-exclusion chromatography and electron cryomicroscropy. This study represents part of our(More)
Small heat shock proteins usually exist as oligomers and appear to undergo dynamic dissociation/reassociation, with oligomeric dissociation being a prerequisite for their chaperone activities. However, contradictory cases were also reported that chaperone activities could be enhanced with no change or even increase in oligomeric sizes. Using Hsp16.3 as a(More)
Seven compounds were isolated from Alinia officinarum Hance and were identified as beta-sitoterol, 1,7-diphenyl-5-ol-3-heptone, 1-phenyl-7-(3'-methoxyl-4'-hydroxyl) phenyl-5-ol-3-heptone, glandin, kaempferol-4'-methylether and 3,4-dihydroxylbenzoic acid by IR, 1HNMR, 13CNMR, FAB-MS and EA. Among these compounds, 3,4-dihydroxylbenzoic acid was the first time(More)
Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis proposed to form specific trimer-of-trimers structures, acts as a molecular chaperone in vitro. The assembly and re-assembly mechanisms of this oligomeric protein were studied and compared using in vitro transcription/translation and denaturization/renaturization systems. Analysis using a(More)
Citation: Chang ZY, Gu LC. Is the mission to identify all the human proteins achievable?—Commenting on the human proteome draft maps. Unveiling the structure and function of all the proteins a human body produces is undoubtedly a key task for us to better understand ourselves. Although a mission difficult to achieve, this apparently becomes more feasible(More)
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