Literature DB >> 12012437

Selective monitoring of 3 out of 50,000 protein vibrations.

Andreas Barth1.   

Abstract

An important group in a large protein, which is the phosphate group that transiently binds to the Ca2+ transporting ATPase (Ca2+-ATPase) of the sarcoplasmic reticulum membrane, is selectively observed with IR spectroscopy. The three phosphate stretching vibrations stand out from the 50,000 protein vibrations in an isotope exchange experiment where oxygen exchange at the phosphate group is catalyzed by the Ca2+-ATPase. Copyright 2002 Wiley Periodicals, Inc.

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Year:  2002        PMID: 12012437     DOI: 10.1002/bip.10085

Source DB:  PubMed          Journal:  Biopolymers        ISSN: 0006-3525            Impact factor:   2.505


  4 in total

1.  Use of helper enzymes for ADP removal in infrared spectroscopic experiments: application to Ca2+-ATPase.

Authors:  Man Liu; Eeva-Liisa Karjalainen; Andreas Barth
Journal:  Biophys J       Date:  2005-02-24       Impact factor: 4.033

2.  Toward a general method to observe the phosphate groups of phosphoenzymes with infrared spectroscopy.

Authors:  Eeva-Liisa Karjalainen; Amelie Hardell; Andreas Barth
Journal:  Biophys J       Date:  2006-06-23       Impact factor: 4.033

3.  Structural changes in the catalytic cycle of the Na+,K+-ATPase studied by infrared spectroscopy.

Authors:  Michael Stolz; Erwin Lewitzki; Rolf Bergbauer; Werner Mäntele; Ernst Grell; Andreas Barth
Journal:  Biophys J       Date:  2009-04-22       Impact factor: 4.033

4.  The determinants of stability and folding in evolutionarily diverged cytochromes c.

Authors:  Megan C Thielges; Jörg Zimmermann; Philip E Dawson; Floyd E Romesberg
Journal:  J Mol Biol       Date:  2009-03-04       Impact factor: 5.469

  4 in total

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