dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide

National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.

1999

1999

Intrinsic tryptophan fluorescence identifies specific conformational changes at the actomyosin interface upon actin binding and ADP release.

The helix-loop-helix (A-site) and myopathy loop (R-site) are located on opposite sides of the cleft that separates the proposed…

1990

1990

Tryptophan‐130 is the most reactive tryptophan residue in rabbit skeletal myosin subfragment‐1

1987

1987

Modification of myosin subfragment 1 tryptophans by dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide.

Modification of tryptophanyl residues (Trps) of myosin subfragments 1 (S-1) was performed with dimethyl(2-hydroxy-5-nitrobenzyl…