Illustrations

Our Favorite Molecule

Myoglobin according to Brian Hudson

Apomyoglobin

Mapping of the earliest-folded regions of apomyoglobin onto the backbone structure of MbCO.

cylinders: regions that are sampled in the quench-flow experiment. (slowly-exchanging amides in the native state)

dotted lines: regions that are not sampled in the quench-flow experiment.

white: regions that fold slowly (~seconds)

colors: regions that are folded, with amides protected, within the dead time of the quench-flow apparatus (~ 6 ms). These regions are folded first.

Structures

Escherichia coli Thioredoxin

Oxidized Thioredoxin

Jeng et al., Structure, 2, 853-868 (1995)

Reduced Thioredoxin

Jeng et al., Structure, 2, 853-868 (1995)

Thiobacillus ferrooxidans Rusticyanin

Reduced (Cu(I)) Rusticyanin

Botuyan et al., J. Mol. Biol. 263, 752-767 (1996)

Inserted Domain of Human Integrin LFA-1

Legge et al., J. Mol. Biol. 295, 1251-1264 (2000)

Cysteine-Rich Domain of Escherichia coli DnaJ

Martinez-Yamout et al., J. Mol. Biol. 300, 805-818 (2000)

Mouse Doppel Protein, a Prion-Look-Alike

Mo et al., Proc. Natl. Acad. Sci. USA 98, 2352-2357 (2001)

Escherichia coli Glutaredoxin 2, a Glutathione-S-Transferase Look-Alike

Xia et al., J. Mol. Biol. 310, 907-918 (2001)

The Third Immunoglobulin Domain of the Neural Cell Adhesion Molecule NCAM

Atkins et al., J. Mol. Biol. 311, 161-172 (2001)

Zinc-Bound C-terminal Domain of Hsp33

Won et al., J. Mol. Biol. 341, 893-899 (2004)

Quorum Sensing Protein SdiA from Escherichia coli

Yao et al., J. Mol. Biol. 355, 262-273 (2006)