1.
Electronic absorption band assignments for copper (II) salicylaldimine
complexes. T.N. Waters and P.E. Wright (1971) J. Inorg. Nucl. Chem. 33,
359‑363.
2.
Conformational influences in copper co-ordination compounds. Part V.
3.
Outline structure of cytochrome c3
and consideration of its properties. C.M. Dobson, N.J. Hoyle,
C.F. Geraldes, M. Bruschi, J. LeGall, P.E. Wright and
R.J.P. Williams (1974) Nature 249, 425-429.
4.
E.S.R. and optical spectral properties of copper (II) complexes with Schiff
base ligands derived from o-amino-benzaldehyde. G.A. Bowmaker,
T.N. Waters and P.E. Wright (1975) J. Chem. Soc. Dalton, 867-870.
5.
Electronic transitions in salicylaldimine complexes. A.C. Braithwaite,
P.E. Wright and T.N. Waters (1975) J. Inorg. Nucl. Chem. 37,
1669-1674.
6.
Assignment of NMR spectrum of iron (III) protoporphyrin (IX) dicyanide using
paramagnetic shift and broadening probes. J.G. Brassington,
R.J.P. Williams and P.E. Wright (1975) J.C.S. Chem. Commun., 338-340.
7.
Conformational studies of peroxidase-substrate complexes. Structure of the
indolepropionic acid-horseradish peroxidase complex. P.S. Burns,
R.J.P. Williams and P.E. Wright (1975) J.C.S. Chem. Commun., 795-796.
8.
Proton magnetic resonance studies of peroxidases from turnip and horseradish. R.J.P. Williams,
P.E. Wright, G. Mazza and J.R. Ricard (1975) Biochim. Biophys. Acta 412, 127-147.
9.
Pulse methods for the simplification of protein NMR spectra. I.D. Campbell,
C.M. Dobson, R.J.P. Williams and P.E. Wright (1975) FEBS Lett. 57, 96-99.
10.
A study of redox reactions of biological importance between Fe (III) complexes
and aromatic moieties. P.S. Burns, J.F. Harrod, R.J.P. Williams
and P.E. Wright (1976) Biochim.
Biophys. Acta 428, 261-268.
11.
Nuclear magnetic resonance studies of the adrenal gland and some other organs. A. Daniels,
R.J.P. Williams and P.E. Wright (1976) Nature 261, 321-322.
12.
High resolution NMR studies of soybean leghemoglobin a. P.E. Wright and
13.
Oxidation and reduction properties of cytochromes and peroxidases. R.J.P. Williams,
G.R. Moore and P.E. Wright, (1977) In: Biological Aspects of Inorganic Chemistry., Eds. A.W. Addison,
W.R. Cullen, D. Dolphin and B.R. James, Wiley, New York,
369-401.
14.
The proton NMR spectra of whole organs. A. Daniels, J. Krebs,
B.A. Levine, P.E. Wright and R.J.P. Williams, (1977) In: NMR in Biology, Eds. R.A. Dwek,
I.D. Campbell, R.E. Richards and R.J.P. Williams, Academic
Press, 277-287.
15.
The storage of small molecules in the octopus salivary gland: nuclear magnetic
resonance study. A. Daniels, J. Krebs, P.E. Wright and R.J.P. Williams
(1977) Biochem. Soc. Trans. 5, 1149-1151.
16.
High resolution proton magnetic resonance studies of plastocyanin. H.C. Freeman,
V.A. Norris, J.A.M. Ramshaw, and P.E. Wright (1977) In: Proceedings of the Fourth International
Congress of Photosynthesis, 805-809.
17.
High resolution proton magnetic resonance studies of plastocyanin. H.C. Freeman,
V.A. Norris, J.A.M. Ramshaw and P.E. Wright (1978) FEBS Lett. 86, 131-135.
18.
The character of stored molecules in chromaffin granules of the adrenal medulla:
a nuclear magnetic resonance study. A.J. Daniels, R.J.P. Williams and
P.E. Wright (1978) Neurosc. 3, 573-585.
19.
Spin state equilibria in soybean ferric leghemoglobin and its complexes with
formate and acetate. J. Trewhella, P.E. Wright and
20.
Molecular basis for proton-dependent anion binding by soybean leghemoglobin a. J. Trewhella, P.E. Wright
and
21.
Conformation and dynamics of biological macromolecules in solution. P.E. Wright
(1979) Proc. Aust. Soc. Biophysics 3, 1S-5S.
22.
Electron transfer reagent binding site on plastocyanin. D.J. Cookson,
M.T. Hayes and P.E. Wright (1980) Nature
283, 682-683.
23.
NMR study of the interactions of plastocyanin with chromium (III) analogues of
inorganic electron transfer reagents. D.J. Cookson, M.T. Hayes and
P.E. Wright (1980) Biochim. Biophys.
Acta. 591, 162-176.
24.
1H NMR and EPR studies on skeletal muscle
actin indicate that the metal and nucleotide binding sites are separate. J.A. Barden,
R. Cooke, P.E. Wright and C.G. dos Remedios (1980) Biochemistry 19, 5912-5916.
25.
1H NMR studies of ferric soybean
leghemoglobin. Assignment of hyperfine shifted resonances of complexes with
cyanide, nictinate, pyridine and azide. J. Trewella and P.E. Wright
(1980) Biochim. Biophys. Acta 625, 202-220.
26.
Resonance Raman evidence for constrained heme structure in soybean
leghemoglobin and its derivatives. R.A. Armstrong, M.J. Irwin and
P.E. Wright (1980) Biochem. Biophys.
Res. Commun. 95, 682-689.
27.
Measurement of heme accessibility in soybean ferric leghemoglobin a and its complexes by proton magnetic
relaxation. D.L. Ollis, P.E. Wright, J.M. Pope and
28.
Heme pocket structure, conformational mobility and heme accessibility of
soybean leghemoglobin. P.E. Wright and C.A. Appleby, 1981 in Current Perspectives in Nitrogen Fixation,
Eds. A.H. Gibson and W.E. Newton, Australian Academy of Science, 365.
29.
Resonance Raman studies of soybean leghemoglobin and myoglobin. Origin of the
differences in O2 dissociation
rate constants. M.J. Irwin, R.S. Armstrong and P.E. Wright
(1981) FEBS Lett. 133, 239-243.
30.
Molecular basis for the pH-dependent binding of O2
to soybean leghemoglobin. P.E. Wright and
31.
Soret excited resonance Raman spectrum of carbonmonoxleghemoglobin: assignment
of uFe-CO.
R.S. Armstrong, M.J. Irwin and P.E. Wright (1982) J. Amer. Chem. Soc. 104, 626-627.
32.
Differences in the heme environment of soybean leghemoglobin components shown
by 1H NMR spectroscopy.
33.
The mobile distal histidine of leghemoglobin: Does it control oxygen binding
kinetics? C.A. Appleby, W.E. Blumberg, J.H. Bradbury,
W.H. Fuchsman, J. Peisach, B.A. Wittenberg, J.B. Wittenberg
and P.E. Wright (1982) In: Interactions
Between Iron and Proteins in Oxygen and Electron Transport, Ed. C. Ho,
Elsevier, 435-441.
34.
A comment on resonance Raman spectroscopic investigations of axial ligation of
the heme iron atom in soybean leghemoglobin a.
R.S. Armstrong, M.J. Irwin, J.E. Wellington and P.E. Wright
(1982) Acta Chem. Scand. 36B, 263-265.
35.
A two-dimensional NMR method for assignment of imidazole ring proton resonances
of histidine residues in proteins. G. King and P.E. Wright (1982) Biochem. Biophys. Res. Commun. 106, 559-565.
36.
13C NMR studies of chlorophyll biosynthesis
in higher plants: an unequivocal proof of the participation of the C5
pathway and evidence of a new route for the incorporation of glycine. R.J. Porra,
O. Klein and P.E. Wright (1982) Biochem.
Internat. 5, 345-350.
37.
1H NMR studies of complexes of ferric
leghemoglobin with substituted pyridines and nicotinic acids. B.C. Mabbutt
and P.E. Wright (1983) J. Inorg.
Biochem. 18, 123-132.
38.
Leghemoglobin. Kinetic, NMR and optical studies of pH dependence of oxygen and
carbon monoxide binding. C.A. Appleby, J.H. Bradbury,
R.J. Morris, B.A. Wittenberg, J.B. Wittenberg and
P.E. Wright (1983) J. Biol. Chem.
258, 2254‑2259.
39.
Assignment of heme and distal amino acid proton resonances in the NMR spectra
of the oxygen and carbonmonoxide complexes of soybean leghemoglobin. B.C. Mabbutt
and P.E. Wright (1983) Biochim.
Biophys. Acta 744, 281-290.
40.
A proton NMR study of the conformation of Trp-Gly-Ala-Glu in
dimethylsulphoxide. G.R. Beilharz, P. Mack, A.V. Robertson and
P.E. Wright (1983) Aust. J. Chem.
36, 751-758.
41.
NMR studies of oxyleghemoglobin. Assignment of distal histidine proton
resonances and evidence for pH-dependent changes in conformation. B.C.
42.
Applications of two-dimensional relayed coherence transfer experiments to 1H
NMR studies of macromolecules. G. King and P.E. Wright (1983) J. Mag. Res. 54, 328-332.
43.
The proof by 13C NMR spectroscopy of
the predominance of the C5 pathway over
the Shemin pathway in chlorophyll biosynthesis in higher plants and of the formation
of the methyl ester group of chlorophyll from glycine. R.J. Porra,
O. Klein and P.E. Wright (1983) Eur.
J. Biochem. 130, 509-516.
44.
An examination of the basic blue copper protein from cucumber peelings by 1H
NMR. G. King, T.A. Andary, H.C. Freeman, L. Gavrilovic and
P.E. Wright (1984) FEBS Lett. 166, 288-292.
45.
Unequivocal proof of chlorophyll formation by the C5
pathway and tenative evidence for Shemin pathway activity in greening leaves. Is
mitochondrial haem formed by the Shemin pathway in leaf cells? R.J. Porra,
O. Klein and P.E. Wright (1984), In: Advances in Photosynthesis Research, Eds. C. Sybesma,
M. Nijhoff, and W. Junk, Vol. IV, 6.725-6.728.
46.
NMR studies of myelin basic protein - XI. Conformation of a nona-peptide from a
segment encephalitogenic in Rhesus monkey. G.L. Mendz, W.J. Moore,
G. King and P.E. Wright (1984) Int.
J. Peptide Protein Chem. 24,
208-217.
47.
Assignment of acyl chain resonances from membranes of mammalian cells by two
dimensional methods. K.J. Cross, K.T. Holmes, C.E. Mountford and
P.E. Wright (1984) Biochemistry 23, 5895-5897.
48.
NMR and kinetic characterization of the interaction between French bean
plastocyanin and horse cytochrome c. G.C. King,
R.A. Binstead and P.E. Wright (1985) Biochim. Biophys. Acta 806,
262-271.
49.
1H NMR studies of the conformation of
eosinophil chemotactic tetra-peptides and analogues in DMSO. G.R. Beilharz,
J.A. Smith, K.F. Austen and P.E. Wright (1985) Int. J. Peptide Protein Chem. 25, 337-346.
50.
NMR studies of the structure and dynamics of monomeric hemoglobins and
myoglobins. P.E. Wright, R.M. Cooke, K.J. Cross,
B.C. Mabbutt, B.A. Messerle and J.E. Wellington (1985) In:
Magnetic Resonance in Biology and
Medicine, Eds. G. Govil, C.L. Khetrapal and A. Saran, Tata-McGraw-Hill, New
Delhi, 131-150.
51.
Calibration of ring current models for the heme ring. K.J. Cross and
P.E. Wright (1985) J. Magn. Res.
64, 220-231.
52.
Acid dissociation constants for plastocyanin in the Cu(I) state. J.D. Sinclair‑Day,
M.J. Sisley, A.G. Sykes, G.C. King and P.E. Wright (1985) Chem. Comm. 505-507.
53.
Conformational disorder of the distal leucine in monomeric Glycera hemoglobins and implications for oxygen binding. R.M. Cooke
and P.E. Wright (1985) FEBS. Lett. 187, 219-223.
54. Completely synthetic vaccine effective
against heterologous enterotoxigenic Escherichia
coli. R.A.van Houghten, R.A. Lerner, S.R. Hoffman,
P.A. Worrell, P.E. Wright and F.A. Klipstein (1985), In: Vaccines 1985. Molecular and Chemical Basis
of Resistance to Parasitic, Bacterial and Viral Diseases, Eds.
R.A. Lerner, R.M. Chanock and F. Brown, Cold Spring Harbor
Laboratory, New York, 91-94.
55.
Simplification of 1H NMR spectra
of proteins by one-dimensional multiple quantum filtration. M. Rance,
C. Dalvit and P.E. Wright (1985) Biochem.
Biophys. Res. Commun. 131,
1094-1102.
56.
Assignment of heme and distal amino acid resonances in the 1H
NMR spectra of the carbon monoxide and oxygen complexes of sperm whale
myoglobin. B.C. Mabbutt and P.E. Wright (1985) Biochim. Biophys. Acta 832,
175-185.
57.
The immunodominant site of a synthetic immunogen has a conformational
preference in water for a type II reverse turn. H.J. Dyson,
K.J. Cross, R.A. Houghten, I.A. Wilson, P.E. Wright and
R.A. Lerner (1985) Nature 318, 480-483.
58.
Antipeptide antibodies and the disorder-order phenomenon. P.E. Wright,
H.J. Dyson, M. Rance, J. Ostresh, R.A. Houghten,
I.A. Wilson and R.A. Lerner (1986), In: New Approaches to Immunization, Eds. R.M. Chanock,
F. Brown and R.A. Lerner, Cold Spring Harbor Press, New York, 15-19.
59.
Differences in amino acid composition and heme electronic structure of the
multiple monomeric hemoglobin components of Glycera
dibranchiata. R.M. Cooke and P.E. Wright (1985) Biochim. Biophys. Acta 832, 357-364.
60.
Heme orientation in the major monomeric hemoglobins of Glycera dibranchiata. R.M. Cooke and P.E. Wright (1985) Biochim. Biophys. Acta 832, 357-372.
61.
Selection by site-directed antibodies of small regions of peptides which are
ordered in water. H.J. Dyson, K.J. Cross, J. Ostresh, R.A. Houghten,
I.A. Wilson, P.E. Wright and R.A. Lerner (1986), In: Synthetic Peptides as Antigens, Ciba
Foundation Symposium 119, John Wiley & Sons, Chichester, pp. 58-75.
62.
Analysis of 1H NMR spectra of
proteins using multiple quantum coherence. M. Rance and P.E. Wright
(1986) J. Magn. Res. 66, 372-378.
63.
1H NMR studies of high spin complexes of
soybean leghemoglobin. Interactions between the distal histidine and acetate,
formate and fluoride ligands. J.
64.
Assignment of methylene resonances in NMR spectra of of cancer cells to plasma
membrane triglyceride. G.L. May, L.C. Wright, K.T. Holmes,
P.G. Williams, I.C.P. Smith, P.E. Wright, R.M. Fox and
C.E. Mountford (1986) J. Biol. Chem.
261, 3048-3053.
65.
Selection rule violations in multiple quantum NMR spectroscopy. M. Rance
and P.E. Wright (1986) Chem. Phys.
Lett. 124, 572-575.
66.
Proton NMR studies of plastocyanin: Assignment of aromatic and methyl group
resonances from 2D spectra. G. King and P.E. Wright (1986) Biochemistry 25, 2364-2374.
67.
Differentiation of direct and remote connectivities in phase sensitive double
quantum spectra of proteins by variation of the multiple quantum excitation
period. C. Dalvit, M. Rance and P.E. Wright (1986) J. Magn. Reson. 69, 356‑361.
68.
1H NMR studies of heme pocket conformation
in zinc-substituted leghemoglobin, a diamagnetic analogue of
deoxyleghemoglobin. C. Dalvit, L. Tennant and P.E. Wright (1986)
J. Inorg. Biochem. 28, 303-309.
69.
The order-disorder paradox in antigen-antibody union: anti-peptide antibodies
as a probe for structured regions of small peptides. H.J. Dyson,
M. Rance, R.A. Houghten, P.E. Wright and R.A. Lerner
(1987), In: Biological
Organization: Macromolecular Interactions at High Resolution, Eds.
R.M. Burnett and H.J. Vogel, Academic Press, pp. 227-234.
70.
Kinetic and mechanisms of the oxidation of myoglobin by Fe(III) and Cu(II)
complexes. K. Hegetschweiler, P. Saltman, C. Dalvit and
P.E. Wright (1987) Biochim. Biophys.
Acta 912, 384-397.
71.
Detection of long-range couplings in proteins via double quantum spectroscopy:
Connection of alphatic and imidazole resonances of histidine residues. C. Dalvit,
P.E. Wright and M. Rance (1987) J.
Magn. Reson. 71, 539-543.
72.
Assignment of resonances in the 1H
NMR spectrum of the carbon monoxide complex of sperm whale myoglobin by phase
sensitive two-dimensional techniques. C. Dalvit and P.E. Wright (1987) J. Mol. Biol. 194, 313-327.
73.
Assignment of resonances in the 1H
NMR spectrum of the carbon monoxide complex of human hemoglobin a-chains. C. Dalvit and
P.E. Wright (1987) J. Mol.
Biol. 194, 329-339.
74.
Site-selective observation of nuclear Overhauser effects in proteins via
isotopic labelling. M. Rance, P.E. Wright, B.A. Messerle and
L.D. Field (1987) J. Am. Chem. Soc.
109, 1591-1593.
75.
1H resonances of proximal histidine in CO
complexes of hemoglobins provide a sensitive probe of coordination geometry. C. Dalvit,
L. Tennant and P.E. Wright (1987) FEBS
Lett. 213, 289-292.
76.
A modified approach to identification of 1H
spin systems in proteins. W.J. Chazin and P.E. Wright (1987) Biopolymers 26, 973-977.
77.
Identification of folded structures in immunogenic peptides by 2D NMR
spectroscopy. P.E. Wright, H.J. Dyson, M. Rance, R.A. Houghten
and R.A. Lerner (1987), In: Protides
of the Biological Fluids, Ed. H. Peeters, Vol. 35, Pergamon Press,
Oxford, pp. 477-480.
78.
NMR studies of the heme pocket conformations of monomeric hemoglobins from Glycera dibranchiata. Implications for
ligand binding. R.M. Cooke, C. Dalvit, S.S. Narula and
P.E. Wright (1987) Eur. J. Biochem.
166, 399-408.
79.
Structural consequences of heme isomerism in monomeric hemoglobins from Glycera dibranchiata. R.M. Cooke
and P.E. Wright (1987) Eur. J.
Biochem. 166, 409-414.
80.
Kinetic studies on 1:1 electron-transfer reactions involving blue copper
proteins. Part 15. The reactivity of Anabaena
variabilis plastocyanin with inorganic complexes and related NMR studies. M.P. Jackman,
J.D. Sinclair-Day, M.J. Sisley, A.G. Sykes, L.A. Denys and
P.E. Wright (1987) J. Amer. Chem.
Soc. 109, 6443-6449.
81.
Complete assignment of lysine resonances in 1H
NMR spectra of proteins as probes of surface structure and dynamics. W.J. Chazin,
M. Rance and P.E. Wright (1987) FEBS
Lett. 222, 109-114.
82.
Electron transfer from cytochrome b5
to iron and copper complexes. L.S. Reid, H.B. Gray, C. Dalvit,
P.E. Wright and P. Saltman (1987) Biochemistry
26, 7102‑7107.
83.
Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence
requirements for the formation of a reverse turn. H.J. Dyson,
M. Rance, R.A. Houghten, R.A. Lerner and P.E. Wright (1988)
J. Mol. Biol. 201, 161-200.
84.
Folding of immunogenic peptide fragments of proteins in water solution. II. The
nascent helix. H.J. Dyson, M. Rance, R.A. Houghten,
P.E. Wright and R.A. Lerner (1988) J. Mol. Biol. 201,
201-217.
85.
The physical basis induction of protein-reactive anti-peptide antibodies. H.J. Dyson,
R.A. Lerner and P.E. Wright (1988) Ann. Rev. Biophysics Biophys. Chem. 17, 305-324.
86. Kinetic studies on 1:1 electron transfer
reactions involving blue copper proteins. 16. The reactivity of plastocyanin
from the green alga Scenedesmus obliquus
with inorganic redox partners and related NMR studies. J. McGinnis,
J.D. Sinclair‑Day, A.G. Sykes, R. Powls, J. Moore and
P.E. Wright (1988) Inorg. Chem. 27, 2306-2312.
87.
Complete assignment of the 1H NMR spectrum
of French bean plastocyanin: application of an integrated approach to spin
system identification in proteins. W.J. Chazin, M. Rance and
P.E. Wright (1988) J. Mol. Biol.
202, 603-622.
88.
Complete assignment of the 1H NMR spectrum
of French bean plastocyanin: sequential resonance assignments, secondary
structure and global fold. W.J. Chazin and P.E. Wright (1988) J. Mol. Biol. 202, 623-636.
89.
Structural differences between oxidized and reduced thioredoxin monitored by
two-dimensional 1H NMR
spectroscopy. H.J. Dyson, A. Holmgren and P.E. Wright (1988) FEBS Lett. 228, 254-258.
90.
Three-dimensional solution structure of plastocyanin from the green alga Scenedesmus obliquus. J.M. Moore,
D.A. Case, W.J. Chazin, G.P. Gippert, T.F. Havel,
R. Powls and P.E. Wright (1988) Science
240, 314-317.
91.
Conformation of peptide fragments of proteins in aqueous solution: implications
for initiation of protein folding. P.E. Wright, H.J. Dyson and
R.A. Lerner (1988) Biochemistry 27, 7167-7175.
92.
1H NMR studies of plastocyanin from Scenedesmus obliquus: Complete
sequence-specific assignment, secondary structure analysis and global fold. J.M. Moore,
W.J. Chazin, R. Powls and P.E. Wright (1988) Biochemistry 27, 7806‑7816.
93.
1H NMR studies of human C3a anaphylatoxin
in solution: sequential resonance assignments, secondary structure and global
fold. W.J. Chazin, T.E. Hugli and P.E. Wright (1988) Biochemistry 27, 9139-9148.
94.
Isotope-edited NMR studies of Fab-peptide complexes. P. Tsang,
T.M. Fieser, R.A. Houghten, R.A. Lerner and P.E. Wright
(1988) Pept. Res. 1, 87-92.
95.
NMR studies of the conformations of leghemoglobins from soybean and lupin. S.S. Narula,
C. Dalvit,
96.
Multiple Quantum NMR. M. Rance, W.J. Chazin, C. Dalvit and
P.E. Wright (1989), In: Methods
in Enzymology, Eds. N. Oppenheimer and T.L. James, Vol. 176, 114-134.
97.
Chemical modification of bovine pancreatic trypsin inhibitor for single site
coupling of immunogenic peptides for NMR conformational analysis. S. Ebina,
R.A. Lerner and P.E. Wright (1989) J. Biol. Chem. 264,
7882-7888.
98.
1H NMR studies of the solution
conformations of an analogue of the C-peptide of ribonuclease A. J.J. Osterhout, Jr.,
R.L. Baldwin, E.J. York, J.M. Stewart, H.J. Dyson and
P.E. Wright (1989) Biochemistry 28, 7059-7064.
99.
Folding of peptide fragments of proteins in water solution. P.E. Wright,
H.J. Dyson and R.A. Lerner (1989), In: Protein Folding. Deciphering the Second Half of the Genetic Code,
Eds. J.A. King and L.M. Gierasch, AAAS,
95-102.
100. Assignment of the proton NMR spectrum of
reduced and oxidized thioredoxin: sequence-specific assignments, secondary
structure and global fold. H.J. Dyson, A. Holmgren and
P.E. Wright (1989) Biochemistry 28, 7074-7087.
101. Folding of peptide fragments of proteins in
aqueous solution. P.E. Wright, H.J. Dyson, V.A. Feher,
L. Tennant, J.P. Waltho, R.A. Lerner and D.A. Case (1990), In:
Frontiers of NMR in Molecular Biology,
UCLA Symposia on Molecular and Cellular Biology, New Series, Eds. D. Live,
I. Armitage and D. Patel, Vol. 109, Alan R. Liss, Inc., New York,
1-13.
102. Solution NMR studies of Fab'-peptide complexes.
P. Tsang, T.M. Fieser, J.M. Ostresh, R.A. Houghten,
R.A. Lerner and P.E. Wright (1990) In: Frontiers of NMR in Molecular Biology, UCLA Symposia on Molecular
and Cellular Biology, New Series, Eds. D. Live,
103. Conformation of a T cell stimulating peptide in
aqueous solution. J.P. Waltho, R.A. Lerner and P.E. Wright
(1989) FEBS Lett. 250, 400-404.
104. What can two-dimensional NMR tell us about
proteins? P.E. Wright (1989) Trends
Biochem. Sci. 14, 255-260.
105. Three-dimensional solution structure of a
single zinc finger DNA-binding domain. M.S. Lee, G.P. Gippert,
K.V. Soman, D.A. Case and P.E. Wright (1989) Science 245, 635-637.
106. Complete assignment of the 1H
nuclear magnetic resonance spectrum of a synthetic zinc finger from Xfin. Sequential resonance assignments
and secondary structure. M.S. Lee, J. Cavanagh and P.E. Wright
(1989) FEBS Lett. 254, 159‑164.
107. Folding of peptide fragments of proteins in
water solution: implications for initiation of protein folding. P.E. Wright,
R.A. Lerner and H.J. Dyson (1989), in Advances in Protein Design, Eds. H. Blocker, J. Collins,
R.D. Schmid, D. Schomburg, VCH Publishers, 13-19.
108. Three-dimensional solution structure of the
reduced form of Escherichia coli
thioredoxin determined by NMR spectroscopy. H.J. Dyson, G.P. Gippert,
D.A. Case, A. Holmgren and P.E. Wright (1990) Biochemistry 29, 4129-4136.
109. Proton Nuclear Magnetic Resonance assignments
and solution structure of a synthetic zinc finger from Xfin. M.S. Lee, G.P. Gippert, K.V. Soman,
D.A. Case and P.E. Wright (1990), In: Proceedings of Sixth
Conversation in Biomolecular Stereodynamics.
Structure and Methods: Volume 2, DNA-Protein Complexes and Proteins, Eds.
R.H. Sarma and M.H. Sarma, Adenine Press, Albany, NY, 83-91.
110. Computational methods for determining protein
structures from NMR data. G.P. Gippert, P.F. Yip, P.E. Wright
and D.A. Case (1990) Biochem.
Pharmacol. 40, 15-22.
111. The H-helix of myoglobin as a potential
independent protein folding domain. J.P. Waltho, V.A. Feher and
P.E. Wright (1990), In: Current
Research in Protein Chemistry: Techniques, Structure and Function, The
Protein Society, Ed. J.J. Villafranca, Academic Press, San Diego, 283-293.
112. Antigen-antibody interactions: an NMR approach.
P.E. Wright, H.J. Dyson, R.A. Lerner, L. Riechmann and
P. Tsang. (1990) Biochem. Pharmacol.
40, 83‑88.
113. Conformational preferences of synthetic
peptides derived from the immunogenic site of the circumsporozoite protein of Plasmodium falciparum by 1H
NMR. H.J. Dyson, A.C. Satterthwait, R.A. Lerner and
P.E. Wright (1990) Biochemistry 29, 7828-7837.
114. Signal suppression in the frequency domain to
remove undesirable resonances with dispersive lineshapes. P. Tsang,
P.E. Wright and M. Rance (1990) J. Magn. Reson.
88, 210-215.
115. Structural characterization of a partly folded
apomyoglobin intermediate. F.M. Hughson, P.E. Wright and
R.L. Baldwin (1990) Science 249, 1544-1548.
116. 1H
NMR assignments of the Escherichia coli
dihydrofolate reductase complex with folate: Evidence for a unique conformation
of bound folate. C.J. Falzone, S.J. Benkovic and P.E. Wright
(1990) Biochemistry 29, 9667-9677.
117. Specific deuteration strategy for enhancing
direct nuclear Overhauser effects in high molecular weight complexes. P. Tsang,
P.E. Wright and M. Rance (1990) J. Amer.
Chem. Soc. 112, 8183-8185.
118. The conformational restriction of synthetic
vaccines for malaria. A.C. Satterthwait, L.-C. Chiang, T. Arrhenius,
E. Cabezas, F. Zavala, H.J. Dyson, P.E. Wright and
R.A. Lerner (1990) Bull. World Hlth
Organiz. 68 (Suppl), 17‑25.
119. Zinc is required for folding and binding of a
single zinc finger to DNA. M.S. Lee, J.M. Gottesfeld and
P.E. Wright (1991) FEBS Lett. 279, 289-294.
120. Sensitivity improvement in proton-detected
two-dimensional heteronuclear relay spectroscopy. J. Cavanagh,
A.G. Palmer III, P.E. Wright & M. Rance (1991) J. Magn. Reson. 91, 429-436.
121. Isotope-edited nuclear magnetic resonance studies
of Fab-peptide complexes. P. Tsang, M. Rance and P.E. Wright
(1991) In: Methods in Enzymology,
Vol. 203, 241-261.
122. The three-dimensional solution structure of
human anaphylatoxin C3a. M.W. Kalnik, W.J. Chazin and
P.E. Wright (1991) In: Techniques
in Protein Chemistry II, Ed. J.J. Villafranca, Academic Press,
123. Defining solution conformations of small linear
peptides. H.J. Dyson and P.E. Wright (1991) Ann. Rev. Biophysics Biophys. Chem. 20, 519-538.
124. Kinetics and mechanism of reduction of Cu(II)
and Fe (III) complexes by soybean leghemoglobin a. D.A. Bakan, P. Saltman, Y. Theriault and
P.E. Wright (1991) Biochim. Biophys.
Acta, 1079, 182-196
125. Mapping the anatomy of the immunodominant
domain of the HIV GP41 transmembrane protein: Peptide conformation analysis
using monoclonal antibodies and proton nuclear magnetic resonance spectroscopy.
M.B.A. Oldstone, A. Tishon, H. Lewicki, H.J. Dyson,
V.A. Feher, N. Assa-Munt and P.E. Wright (1991) J. Virol. 65, 1727-1734.
126. Evidence for two interconverting protein
isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coli. C.J. Falzone,
P.E. Wright and S.J. Benkovic (1991) Biochemistry 30,
2184-2191.
127. Sensitivity improvement in proton detected two-dimensional
heteronuclear correlation NMR spectroscopy. A.G. Palmer III.
J. Cavanagh, P.E. Wright and M. Rance (1991) J. Magn. Reson. 93, 151-170.
128. Intramolecular motions of a zinc finger
DNA-binding domain from Xfin
characterized by proton-detected natural abundance 13C
heteronuclear NMR spectroscopy. A.G. Palmer III, M. Rance and
P.E. Wright (1991) J. Amer. Chem. Soc. 113, 4371-4380.
129. Polypeptide backbone resonance assignments and
secondary structure of Bacillus subtilis
enzyme IIIglc determined by
two-dimensional and three-dimensional heteronuclear NMR spectroscopy. W.J. Fairbrother,
J. Cavanagh, H.J. Dyson, A.G. Palmer, S.L. Sutrina,
J. Reizer, M.H. Saier, and P.E. Wright (1991) Biochemistry 30, 6896-6907.
130. Measurement of relaxation rate constants for
methyl groups by proton-detected heteronuclear NMR spectroscopy. A.G. Palmer III,
P.E. Wright and M. Rance (1991) Chem.
Phys. Lett. 185, 41-46.
131. High-resolution solution structure of reduced
French bean plastocyanin and comparison with the crystal structure of poplar
plastocyanin. J.M. Moore, C. Lepre, G.P. Gippert,
W.J. Chazin, D.A. Case and P.E. Wright (1991) J. Mol. Biol. 221, 533-555.
132. Solution structures of DNA-binding domains of
eukaryotic transcription factors. P.E. Wright (1992) In: Transcriptional Regulation, Eds.
K. Yamamoto and S. McKnight,
133. Suppression of the effects of cross-correlation
between dipolar and anisotropic chemical shift relaxation mechanisms in the
measurement of spin-spin relaxation rates. A.G. Palmer III,
N.J. Skelton, W.J. Chazin, P.E. Wright and M. Rance (1992) Mol. Phys., 75, 699-711.
134. A comparison of the requirements for pre-formed
secondary structure in proteins with different structures in the folded state. H.J. Dyson
and P.E. Wright (1992) In: Proceedings of Seventh Conversation in
Biomolecular Stereodynamics. Structure
and Function, Volume 2:Proteins, Eds. R.H. Sarma and M.H. Sarma,
Adenine Press,
135. Specific interactions of the first three zinc
fingers of TFIIIA with the internal control region of the Xenopus 5S RNA gene. X. Liao, K. Clemens,
L. Tennant, P.E. Wright and J. Gottesfeld (1992) J. Mol. Biol. 223, 857-871.
136. Immunogenic peptides corresponding to the
dominant antigenic region alanine-597 to cysteine-619 in the transmembrane
protein of simian immunodeficiency virus have a propensity to fold in aqueous
solution. H.J. Dyson, E. Norrby, K. Hoey, D.E. Parks,
R.A. Lerner and P.E. Wright (1992) Biochemistry 31, 1458‑1463.
137. Improved resolution in three-dimensional
constant-time triple resonance NMR spectroscopy of proteins. A.G. Palmer III,
W.J. Fairbrother, J. Cavanagh, P.E. Wright and M. Rance
(1992) J. Biomol. NMR 2, 103-108.
138. Low resolution solution structure of the Bacillus subtilis glucose permease IIA
domain derived from heteronuclear three-dimensional NMR spectroscopy. W.J. Fairbrother,
G.P. Gippert, J. Reizer, M.H. Saier Jr. and P.E. Wright
(1992) FEBS Lett. 296, 148-152.
139. Structural determinants of Cys2 His2
zinc fingers. R.J. Mortishire-Smith, M.S. Lee, L. Bolinger and
P.E. Wright (1992) FEBS Lett. 296, 11-15.
140. Folding of peptide fragments comprising the
complete sequence of proteins: Models
for initiation of protein folding. I. Myohemerythrin. H.J. Dyson,
G. Merutka, J.P. Waltho, R.A. Lerner and P.E. Wright (1992) J. Mol. Biol. 226, 795‑817.
141. Folding of peptide fragments comprising the
complete sequence of proteins:Models for initiation of protein folding. II.
Plastocyanin. H.J. Dyson, J.R. Sayre, H-C. Shin,
G. Merutka, R.A. Lerner and P.E. Wright (1992) J. Mol. Biol. 226, 819-835.
142. Relationship between 1H
and 13C NMR chemical shifts
and the secondary and tertiary structure of a zinc finger peptide. M.S. Lee,
A.G. Palmer III and P.E. Wright (1992) J. Biomol. NMR 2,
307-322.
143. Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N
NMR relaxation measurements. M.J. Stone, W.J. Fairbrother,
A.G. Palmer III, J. Reizer, M.H. Saier Jr. and
P.E. Wright (1992) Biochemistry 31, 4394-4406.
144. Assignment of the aliphatic 1H
and 13C resonances of the Bacillus subtilis glucose permease IIA
domain using double- and triple-resonance heteronuclear three-dimensional NMR
spectroscopy. W.J. Fairbrother, A.G. Palmer, III, M. Rance,
J. Reizer, M.H. Saier, Jr. and P.E. Wright (1992) Biochemistry 31, 4413‑4425.
145. Conformation and dynamics of an Fab'-bound
peptide by isotope-edited NMR spectroscopy. P. Tsang, M. Rance,
T.M. Fieser, J.M. Ostresh, R.A. Houghten, R.A. Lerner and
P.E. Wright (1992) Biochemistry 31, 3862-3871.
146. The zinc finger motif: Conservation of chemical
shifts and correlation with structure. M.S.Lee, R.J. Mortishire-Smith, and
P.E. Wright (1992) FEBS Lett. 309, 29-32.
147. Functional role of a mobile loop of Escherichia coli dihydrofolate reductase
in transition state stabilization. L. Li, C.J. Falzone,
P.E. Wright and S.J. Benkovic (1992) Biochemistry 31,
7826-7833.
148. Definition of the binding sites of individual
zinc fingers in the TFIIIA-5S RNA gene complex. K.R. Clemens,
X. Liao, V. Wolf, P.E. Wright and J.M. Gottesfeld (1992) Proc. Natl Acad. Sci. USA 89, 10822-10826.
149. Determination of high resolution NMR structures
of proteins. D.A. Case and P.E. Wright (1993) In: NMR of Proteins, Eds. G.M. Clore
and A.M. Gronenborn, MacMillan, pp. 53-91.
150. Comparison of backbone and tryptophan sidechain
dynamics of reduced and oxidized E. coli
thioredoxin using 15N NMR
relaxation measurements. M.J. Stone, K. Chandrasekhar,
A. Holmgren, P.E. Wright and H.J. Dyson (1993) Biochemistry 32, 426-435.
151. Three-dimensional structures of the central
regulatory proteins of the bacterial phosphotransferase system, HPr and enzyme
IIAglc. Y. Chen,
W.J. Fairbrother and P.E. Wright (1993) J. Cell. Biochem., 51,
75-82.
152. Mapping of the binding interfaces of the
proteins of the bacterial phosphotransferase system, HPr and IIAglc.
Y. Chen, J. Reizer, M.H. Saier, W.J. Fairbrother and
P.E. Wright (1993) Biochemistry 32, 32-37.
153. Assignments of 1H,
15N and 13C
resonances, identification of elements of secondary structure and determination
of the global fold of the DNA binding domain of GAL4. M. Shirakawa,
W.J. Fairbrother, Y. Serikawa, T. Ohkubo, Y. Kyogoku and
P.E. Wright (1993) Biochemistry 32, 2144-2153.
154. Molecular basis for specific recognition of
both RNA and DNA by a zinc finger protein. K.R. Clemens, V. Wolf,
S.J. McBryant, P. Zhang, X. Liao, P.E. Wright and
J.M. Gottesfeld (1993) Science 260, 530-533.
155. The
solution structure of the Oct-1 POU-specific domain reveals a striking
similarity to the bacteriophage l repressor
DNA-binding domain. N. Assa-Munt, R. Mortishire-Smith,
R. Aurora, W.Herr and P.E. Wright (1993) Cell 73, 193‑205.
156. Peptide conformation and protein folding. H.J. Dyson
and P.E. Wright (1993) Curr. Opin.
Struct. Biol.3, 60-65.
157. Structure of the retinoid X receptor a DNA-binding domain: A helix required for homodimeric DNA binding. M.S. Lee, S.A. Kliewer, J. Provencal, P.E. Wright and R.M. Evans (1993) Science