作者: Suparna Sarkar-Banerjee , Sourav Chowdhury , Simanta Sarani Paul , Debashis Dutta , Anisa Ghosh
DOI: 10.1021/ACS.BIOCHEM.6B00390
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摘要: There has been widespread interest in studying early intermediate states and their roles protein folding. The further emphasized the recent literature because of implications for aggregation. Unfortunately, direct kinetic characterization intermediates difficult limited time resolutions offered by techniques heterogeneity folding aggregation landscape. Even equilibrium experiments, could be (a) populations low and/or (b) they lack any specific biochemical or biophysical signatures identification. In this paper, we have used fluorescence correlation spectroscopy to study nature a low-pH state intestinal fatty acid binding protein, small with predominantly β-sheet structure. Our results shown that pH 3 diffuses faster than fo...