Metal Ions, Protein Folding, and Conformational States

2010 ◽  
pp. 3-11
Author(s):  
Cláudio Gomes ◽  
Pernilla Wittung-Stafshede
Keyword(s):  
Protein Folding ◽  
Metal Ions ◽  
Conformational States

Heavy metal ions are potent inhibitors of protein folding

2008 ◽  
Vol 372 (2) ◽  
pp. 341-345 ◽  
Author(s):  
Sandeep K. Sharma ◽  
Pierre Goloubinoff ◽  
Philipp Christen
Keyword(s):  
Heavy Metal ◽  
Protein Folding ◽  
Metal Ions ◽  
Heavy Metal Ions

Probing Protein Folding with Substitution-Inert Metal Ions. Folding Kinetics of Cobalt(III)-Cytochromec

1999 ◽  
Vol 121 (50) ◽  
pp. 11918-11919 ◽  
Author(s):  
F. Akif Tezcan ◽  
Jay R. Winkler ◽  
Harry B. Gray
Keyword(s):  
Protein Folding ◽  
Metal Ions ◽  
Folding Kinetics ◽  
Kinetics Of

scholarly journals Analysis of Protein Folding Equilibria by Nano-Electrospray-Ionization Mass Spectrometry

2002 ◽  
Vol 16 (3-4) ◽  
pp. 361-370 ◽  
Author(s):  
Irena Matecko ◽  
Norbert Müller ◽  
Rita Grandori
Keyword(s):  
Mass Spectrometry ◽  
Protein Folding ◽  
Electrospray Ionization ◽  
Electrospray Ionization Mass Spectrometry ◽  
Tertiary Structure ◽  
Molten Globule ◽  
Ionization Mass Spectrometry ◽  
Ionization Mass ◽  
Conformational States ◽  
Esi Ms

This paper summarizes recent findings from our group concerning applications of electrospray-ionization mass spectrometry (ESI-MS) to the study of protein folding. Nano-ESI-MS was employed for the investigation of protein conformational states under varying solvent conditions and at varying values of the instrumental parameters. The effect of trifluoroethanol (TFE) on a peptide and acid-unfolded cytochromec(cytc), monitored by circular dichroism (CD) and time-of-flight ESI-MS, illustrates the specificity of the latter technique for features of protein tertiary structure. Measurements on marginally stable protein states indicate that it is possible to identify operational conditions for nano-ESI-MS in which none of the instrumental parameters limits conformational stability in the protein sample. Results described here show that changes in the charge-state distributions (CSDs) under controlled conditions allow not only discriminating between native and denatured states, but also monitoring minor conformational changes, like the transition from molten globule to native state. These studies underscore the potential of mass spectrometry methods for the analysis of heterogeneous samples and, in particular, for the characterization of dynamic equilibria involving different conformational states.

Metal ions induced secondary structure rearrangements: mechanically interlocked lassovs.unthreaded branched-cyclic topoisomers

The Analyst ◽  
2018 ◽  
Vol 143 (10) ◽  
pp. 2323-2333 ◽  
Author(s):  
Kevin Jeanne Dit Fouque ◽  
Javier Moreno ◽  
Julian D. Hegemann ◽  
Séverine Zirah ◽  
Sylvie Rebuffat ◽  
...  
Keyword(s):  
Protein Folding ◽  
Secondary Structure ◽  
Metal Ions ◽  
Conformational Change ◽  
Structural Stability ◽  
Significant Role

Metal ions can play a significant role in a variety of important functions in protein systems including cofactor for catalysis, protein folding, assembly, structural stability and conformational change.

Solution Structure of Apo Cu,Zn Superoxide Dismutase:  Role of Metal Ions in Protein Folding†

Biochemistry ◽  
2003 ◽  
Vol 42 (32) ◽  
pp. 9543-9553 ◽  
Author(s):  
Lucia Banci ◽  
Ivano Bertini ◽  
Fiorenza Cramaro ◽  
Rebecca Del Conte ◽  
Maria Silvia Viezzoli
Keyword(s):  
Superoxide Dismutase ◽  
Protein Folding ◽  
Metal Ions ◽  
Solution Structure
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