Institite for Intrinsically Disordered Protein Research, Center for Computational Biology and Bioinformatics, Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Curr Protein Pept Sci. 2009 Oct;10(5):447-55. doi: 10.2174/138920309789352029.
The structure of a globular protein is known to be affected by addition of acids or alkalis. The fact that a protein unfolds or at least denatures in solutions with extreme pH values was known for a long time. Prof. Anthony L. Fink (Tony) brought this field to a new level by showing that acid-unfolded proteins can partially regain their ordered structures in the presence of various anions. This review analyses his contributions to this branch of protein science. His studies provided an explanation for the molecular mechanisms underlying anion-induced refolding of acid-unfolded proteins. He was the first who clearly showed that different anions differed dramatically in their efficiency to bring about this refolding. This difference was shown to be manifested in the amounts of anions needed to complete a structural transition, in the degree of cooperativity of these transitions, and in the amounts of ordered structure induced in the acid-unfolded proteins at the completion of the corresponding transitions. He was also first who undoubtedly demonstrated that, at low pH, proteins can populate discrete partially folded conformations in the presence of different anions. His papers are highly cited, clearly showing that the work of Tony Fink on anion-induced folding of globular proteins made a great impact to the protein folding field.
球状蛋白的结构已知会受到添加酸或碱的影响。很长一段时间以来，人们都知道在极端 pH 值的溶液中，蛋白质会展开或至少变性。安东尼·L·芬克教授（Tony）通过证明在各种阴离子存在的情况下，酸展开的蛋白质可以部分恢复其有序结构，将该领域提升到了一个新的水平。这篇综述分析了他对蛋白质科学这一分支的贡献。他的研究为阴离子诱导酸展开的蛋白质重折叠的分子机制提供了解释。他是第一个明确表明不同阴离子在使这种重折叠的效率上有显著差异的人。这种差异表现在完成结构转变所需的阴离子量、这些转变的协同性程度以及在完成相应转变时在酸展开的蛋白质中诱导的有序结构的量上。他也是第一个毫无疑问地证明，在低 pH 值下，蛋白质可以在不同的阴离子存在下呈现离散的部分折叠构象的人。他的论文被高度引用，清楚地表明 Tony Fink 关于阴离子诱导球状蛋白折叠的工作对蛋白质折叠领域产生了重大影响。
