Thermal and chemical modification of protein structures is known to affect their interfacial activity. We have looked in detail at the effect of heating on the structure and subsequently the surface properties of LTP1, a nonspecific lipid transfer protein from barley, both in the presence and in the absence of its lipid adduct. CD and NMR spectroscopy showed that some of the protein molecules refold back to the native state structure after being heated to 100 degrees C for 2 h. However, for a...Expand abstract
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Partially folded forms of barley lipid transfer protein are more surface active.
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