|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
3
|
|
pubmed:dateCreated |
1993-3-5
|
|
pubmed:abstractText |
For further insight into the role of solvent in protein conformer stabilization, the structural and dynamic properties of protein ions in vacuo have been probed by hydrogen-deuterium exchange in a Fourier-transform mass spectrometer. Multiply charged ions generated by electrospray ionization of five proteins show exchange reactions with 2H2O at 10(-7) torr (1 torr = 133.3 Pa) exhibiting pseudo-first-order kinetics. Gas-phase compactness of the S-S cross-linked RNase A relative to denatured S-derivatized RNase A is indicated by exchange of 35 and 135 hydrogen atoms, respectively. For pure cytochrome c ions, the existence of at least three distinct gaseous conformers is indicated by the substantially different values--52, 113, and 74--of reactive H atoms; the observation of these same values for ions of a number--2, 7, and 5, respectively--of different charge states indicates conformational insensitivity to coulombic forces. For each of these conformers, the compactness in vacuo indicated by these values corresponds directly to that of a known conformer structure in the solution from which the conformer ions are produced by electrospray. S-derivatized RNase A ions also exist as at least two gaseous conformers exchanging 50-140 H atoms. Gaseous conformer ions are isometrically stable for hours; removal of solvent greatly increases conformational rigidity. More specific ion-molecule reactions could provide further details of conformer structures.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1309610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1310539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1411504,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1553543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1609279,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1666527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1666528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1789447,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1883209,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1948083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-1992509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-2177335,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-2552435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-2675315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-2824793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-5459638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8381533-6184480
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
1
|
|
pubmed:volume |
90
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
790-3
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:8381533-Cytochrome c Group,
pubmed-meshheading:8381533-Enzyme Stability,
pubmed-meshheading:8381533-Gases,
pubmed-meshheading:8381533-Ions,
pubmed-meshheading:8381533-Mass Spectrometry,
pubmed-meshheading:8381533-Myoglobin,
pubmed-meshheading:8381533-Protein Conformation,
pubmed-meshheading:8381533-Proteins,
pubmed-meshheading:8381533-Ribonuclease, Pancreatic,
pubmed-meshheading:8381533-Ubiquitins
|
|
pubmed:year |
1993
|
|
pubmed:articleTitle |
Coexisting stable conformations of gaseous protein ions.
|
|
pubmed:affiliation |
Baker Chemistry Laboratory, Cornell University, Ithaca, NY 14853-1301.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
