PROTEIN PROTEIN &PROTEIN DNA INTERACTIONS STUDIED BY CHEMICAL CROSS LINKING

$8,199P41FY2000RRNIH

Rockefeller University, New York NY

Investigators

Linked publications & trials

Paper 33259802 Paper 33049227 Paper 32967858 Paper 32782366 Paper 32289258 Paper 31819269 Paper 31774265 Paper 27693350 Paper 27080007 Paper 26042681 Paper 25667060 Paper 25588722 Paper 25242333 Paper 25086043 Paper 24075807 Paper 23516416 Paper 23306439 Paper 23276924 Paper 23273981 Paper 22860026 Paper 22768092 Paper 22709632 Paper 22474365 Paper 22331846 Paper 22309600 Paper 22244332 Paper 22241783 Paper 22239320 Paper 22129306 Paper 22033520 Paper 22009756 Paper 21893598 Paper 21877294 Paper 21764753 Paper 21642990 Paper 21516228 Paper 21454883 Paper 21390248 Paper 21135131 Paper 21082431 Paper 21050864 Paper 20921377 Paper 20835802 Paper 20835801 Paper 20835799 Paper 20702425 Paper 20585571 Paper 20572018 Paper 20548778 Paper 20504932 Paper 20486120 Paper 20392851 Paper 20212525 Paper 20211137 Paper 20005841 Paper 19966800 Paper 19841479 Paper 19778728 Paper 19628708 Paper 19583196 Paper 19562802 Paper 19525551 Paper 19402746 Paper 19380747 Paper 19270693 Paper 19216906 Paper 19213839 Paper 19151997 Paper 19098896 Paper 18951162 Paper 18834145 Paper 18678709 Paper 18407068 Paper 18363801 Paper 18347735 Paper 18321079 Paper 18294652 Paper 18271525 Paper 18171605 Paper 18083804 Paper 17972917 Paper 17922018 Paper 17919899 Paper 17726112 Paper 17703190 Paper 17668044 Paper 17656582 Paper 17630825 Paper 17360435 Paper 17284592 Paper 17199039 Paper 17157260 Paper 17116750 Paper 16895903 Paper 16885219 Paper 16630816 Paper 16615907 Paper 16461911 Paper 16425180 Paper 16365162

Abstract

The objective of this investigation is to use chemical cross-linking reactions and chemical modification together with mass spectrometric techniques to study the contact interactions between protein-protein and protein-DNA complexes. Various cross-linking and modification reagents have been selected for these investigations. Reagents that probe the accessibilities of a number of amino acid side-chains have been investigated, including His, Try, Lys, and Arg. Our studies have shown that laser desorption MS is very useful in following the nature and extent of reaction. We are currently developing the use of the MALDI-Ion Trap to map the sites of modifications with CAD-MS/MS.

View original record on NIH RePORTER →