Publication Date:
1990-04-13
Description:
Tandem mass spectrometry has been used to obtain information related to portions of the primary sequence for an intact protein, bovine ribonuclease A. Multiply charged molecular ions, generated by electrospray ionization, were collisionally dissociated at low energies in a triple quadrupole mass spectrometer to yield singly and multiply charged fragment ions that can be assigned to the known sequence of the protein. Dissociation of the highly charged molecular ions resulted in pairs of complementary product ions. The higher order (gas-phase) protein structure affects the dissociation processes, as observed in comparisons of tandem mass spectra of the native and disulfide-reduced forms of ribonuclease A.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Loo, J A -- Edmonds, C G -- Smith, R D -- GM 42940/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Apr 13;248(4952):201-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemical Sciences Department, Pacific Northwest Laboratory, Richland, WA 99352.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2326633" target="_blank"〉PubMed〈/a〉
Keywords:
*Amino Acid Sequence
;
Animals
;
Cattle
;
Disulfides
;
Mass Spectrometry/methods
;
Oxidation-Reduction
;
*Proteins
;
*Ribonuclease, Pancreatic
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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