FOCUS: MASS SPECTROMETRY AS A PROBE OF HIGHER ORDER PROTEIN STRUCTURE: RESEARCH ARTICLE BWet^ Versus BDry^ Folding of Polyproline
نویسندگان
چکیده
Liuqing Shi, Alison E. Holliday, Brian C. Bohrer, Doyong Kim, Kelly A. Servage, David H. Russell, David E. Clemmer Department of Chemistry, Indiana University, Bloomington, IN 47405, USA Department of Chemistry, Moravian College, Bethlehem, PA 18018, USA Department of Chemistry, University of Southern Indiana, Evansville, IN 47712, USA Department of Chemistry, Texas A&M University, College Station, TX 77843, USA
منابع مشابه
Ion Mobility-Mass Spectrometry Reveals the Energetics of Intermediates that Guide Polyproline Folding.
Proline favors trans-configured peptide bonds in native proteins. Although cis/trans configurations vary for non-native and unstructured states, solvent also influences these preferences. Water induces the all-cis right-handed polyproline-I (PPI) helix of polyproline to fold into the all-trans left-handed polyproline-II (PPII) helix. Our recent work has shown that this occurs via a sequential m...
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The development of rapid, sensitive, and accurate mass spectrometric methods formeasuring peptides, proteins, and even intact protein assemblies hasmade mass spectrometry (MS) an extraordinarily enabling tool for structural biology. Here, we provide a personal perspective of the increasingly useful role that mass spectrometric techniques are exerting during the elucidation of higher order prote...
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Ion mobility spectrometry (IMS) is increasingly used to describe solution-phase phenomena and has recently been used to establish the presence of multiple intermediates during the folding of a model polypeptide, polyproline. These observations, however, are made on gas-phase structures. Capillary electrophoresis (CE) is a complementary solution-phase technique, also based on the separation of c...
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Mass spectrometry has already become an indispensable tool in the analytical armamentarium of the biopharmaceutical industry, although its current uses are limited to characterization of covalent structure of recombinant protein drugs. However, the scope of applications of mass spectrometry-based methods is beginning to expand to include characterization of the higher order structure and dynami...
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It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...
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تاریخ انتشار 2016