SOLVENT INDUCED CD EFFECTS IN OLIGO (PHEMYLENE ETHYNYLENES)S

$5,819P41FY2000RRNIH

University Of Illinois Urbana-Champaign, Champaign IL

Investigators

Linked publications & trials

Paper 30613865 Paper 29959835 Paper 29572236 Paper 28355163 Paper 28092391 Paper 27480804 Paper 27449340 Paper 25976033 Paper 25684346 Paper 25383253 Paper 25331141 Paper 25152766 Paper 24839062 Paper 24825347 Paper 24802848 Paper 24706556 Paper 24681536 Paper 24610799 Paper 24567663 Paper 24563776 Paper 24561157 Paper 24474217 Paper 24473084 Paper 24376913 Paper 24371363 Paper 24296066 Paper 24270641 Paper 24138850 Paper 24066941 Paper 24040513 Paper 24039347 Paper 24016602 Paper 23935614 Paper 23897846 Paper 23739629 Paper 23684974 Paper 23528083 Paper 23520655 Paper 23510681 Paper 23358889 Paper 23343159 Paper 23304656 Paper 23297401 Paper 23296945 Paper 23278596 Paper 23276538 Paper 23259580 Paper 23248275 Paper 23235925 Paper 23232795 Paper 23224167 Paper 23214184 Paper 23199932 Paper 23144844 Paper 23085915 Paper 23019116 Paper 22891156 Paper 22866180 Paper 22828352 Paper 22824282 Paper 22736488 Paper 22713584 Paper 22665783 Paper 22559690 Paper 22517076 Paper 22415853 Paper 22391890 Paper 22325293 Paper 22298327 Paper 22281872 Paper 22234820 Paper 22216230 Paper 22153505 Paper 22112124 Paper 21980464 Paper 21950942 Paper 21919444 Paper 21858900 Paper 21811627 Paper 21698153 Paper 21642644 Paper 21641311 Paper 21602447 Paper 21593452 Paper 21527997 Paper 21468650 Paper 21462350 Paper 21425242 Paper 21394110 Paper 21281593 Paper 21281572 Paper 21281565 Paper 21147979 Paper 21121261 Paper 21030952 Paper 20835996 Paper 20823232 Paper 20734406 Paper 20672286 Paper 20459248

Abstract

Fluorescence lifetime and differential phase data will be taken on several hydroxy-Trp protein and their normal Trp forms. Measurment on these protein in the presence and absence of DNA will be performed to study the mobility and the spectral changes of the Trp and hydroxy-Trp residue due to DNA binding. This data will help us understand the pertinent conformational changes involved in the protein.

View original record on NIH RePORTER →