| 1981 |
Determination of affinities of amino acid side chains for solvent
water (Wolfenden et al.).30
|
| 1988 |
De novo design of
a globular α-helical
protein capable of adopting a stable, folded structure in aqueous
solution (DeGrado’s lab).855
|
| 1989 |
(i) Laying the ground
for transmembrane protein design through
the solvent-exposed hydrophobic residue exchange, and suggesting that
transmembrane and soluble proteins share similar core structures with
different solvent-exposed residues (Eisenberg and Rees).208
|
| (ii) Use of a short
hydrophilic sequence to solubilize penicillin-binding
protein 5 with the C-terminus truncation for crystallization (Ferrerra
et al.).407
|
| 1993 |
De novo design of soluble four-helix bundle
proteins by the binary patterning of polar and nonpolar amino acids
(Hecht’s lab).856
|
| 1994 |
De novo design of water-soluble
multiheme
proteins (DeGrado’s lab and Dutton’s lab).484
|
| 1997 |
(i) Computer assisted fully automatic sequence design and validation
of soluble FSD-1 protein (Mayo’s lab).857
|
| (ii) All theoretical design of
soluble bacteriorhodopsin (Gibas
and Subramaniam).250
|
| 2000 |
Design of water-soluble variants for phospholamban
thru mutating
lipid facing amino acids (Engel’s lab, Engelman’s lab,
and DeGrado’s lab).43,359,360
|
| 2002 |
(i) Rational
design of water-soluble bacteriorhodopsin with
14.9% sequence change and limited solubility, still required detergents
and lost purple color (not functional) (Engelman’s lab).251
|
| (ii) Conversion of
transmembrane toxin aerolysin to a soluble
complex through single point mutations (Van der Goot’s lab).222
|
| 2003 |
Enhancing solubility at the physiological pH and folding condition
of ankyrin repeat proteins by substituting surface exposed leucine
with arginine (Peng’s lab).444
|
| 2004 |
(i) Design of water-soluble
analogues for potassium channel
KcsA, 160 aa protein (33/160 aa changes equal to 20.6%) that conducted
ion transport (DeGrado’s lab).226
|
| (ii) MscL channel protein solubilization
through the stoichiometric
covalent modification with amphiphiles (Becker and Kochendoerfer).237
|
| 2005 |
Determination of the tetrameric structure for the water-soluble
truncated phospholamban and elucidation of sequence determinants that
defined coiled-coil symmetry (DeGrado’s lab).215
|
| 2006 |
Redesign of
a potassium channel with unknown structure by conservation
pattern analysis (Roosild and Choe).235
|
| 2008 |
Design and NMR structural
study of solubilized KcsA analogue
(33/81 aa changes = 40.7%) (Xu’s lab).234
|
| 2010 |
Design and
X-ray crystal structure analysis of a water-soluble
form of cross-β architecture (Koide’s lab).172
|
| 2012 |
Design and NMR structure determination of water-soluble nicotinic
acetylcholine receptor (23/140 aa changes = ∼17%) (Xu’s
lab).254
|
| 2013 |
(i) Design of truncated water-soluble
human mu opioid receptor
(53/288 aa changes = 18%), detergent still needed for purification
(Saven’s lab and Liu’s lab).262
|
| (ii) Design and functional study of MotB
by transmembrane segment
swapping with leucine zipper (Andrews and Roujeinikova).239
|
| 2014 |
(i) De novo design and X-ray characterization
of water-soluble α-helical barrels with central pore diameter
related to the oligomeric state (Woolfson’s lab).160
|
| (ii) Optimization
on the transmembrane region design of water-soluble
human mu opioid receptor (46/288 aa changes = 16%), with deteriorated
protein performance (Saven’s lab and Liu’s lab).265,266
|
| 2015 |
Development of a protein
(ApoAI*) fusion strategy (SIMPLEx)
to solubilize 10 types of structurally irrelevant transmembrane proteins
(DeLisa’s lab).267
|
| 2016 |
(i) Engineering soluble human
paraoxonase 2 without disturbing
its folding for quorum quenching (Ge’s lab).412
|
| (ii) Design of internal hydrogen
bond networks in water-soluble
concentric coiled-coils (Baker’s lab).365
|
| 2017 |
(i) De novo design of water-soluble variants
of light-harvesting protein maquettes (Moser’s lab).495
|
| (ii) Solubilization
of membrane bound enzyme DsbB with the
SIMPLEx strategy for in vivo and in vitro applications (DeLisa lab).272
|
| 2018 |
(i) Design and crystal
structure determination of water-soluble
coiled-coils (6/25 aa = 24%) that forms super helical cross-α
amyloids (DeGrado’s lab).162
|
| (ii) Use of the QTY code to design five chemokine
receptors
(20–29% aa change) with native-like ligand specificity and Tm (Zhang’s Lab).274
|
| (iii) De novo design of the water-soluble
β-barrel structure with built-in affinity toward fluorescently
activate DFHBI (Baker’s lab).171
|
| 2019 |
(i) Design of water-soluble
GPCR based chimera receptors with
tunable functions and high thermostability (Zhang’s Lab).277
|
| 2020 |
(i) Design of full length water-soluble human mu opioid receptor
with enhanced stability (Saven’s lab and Liu’s lab).264
|
| (ii) Design of truncated
QTY chemokine receptors for the non-full
length native receptor study (Zhang’s Lab).279
|
| (iii) QTY code based partial solubilization
of CXCR4 that retains
cell function (Zhang’s Lab).280
|
