G A Petsko

发表

Protein sequencing by computer graphics.

D Tsernoglou, G A Petsko, A T Tu, 1977, Biochimica et biophysica acta.

Structure and activity of two photoreversible cinnamates bound to chymotrypsin.

G A Petsko, G. Petsko, B. Stoddard, 1990, Biochemistry.

Fluctuations in protein structure from X-ray diffraction.

G A Petsko, G. Petsko, D. Ringe, 1984, Annual review of biophysics and bioengineering.

A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids

P C Babbitt, G L Kenyon, G A Petsko, 1995, Science.

Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.

G A Petsko, G. Petsko, E Lolis, 1990, Biochemistry.

The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate.

G L Kenyon, G A Petsko, G. Petsko, 1994, Biochemistry.

Atomic coordinates for triose phosphate isomerase from chicken muscle.

D W Banner, G A Petsko, G. Petsko, 1976, Biochemical and biophysical research communications.

Computer simulation and analysis of the reaction pathway of triosephosphate isomerase.

M Karplus, G A Petsko, M. Karplus, 1991, Biochemistry.

Analysis of two-residue turns in proteins.

M Karplus, G A Petsko, M. Karplus, 1994, Journal of molecular biology.

Protein crystallography at sub-zero temperatures: cryo-protective mother liquors for protein crystals.

G A Petsko, G. Petsko, 1975, Journal of molecular biology.

Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors.

G A Petsko, G. Petsko, D. Ringe, 1995, Biochemistry.

Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. I5 suggest reasons for thermal instability.

G A Petsko, G. Petsko, A. Szilágyi, 1997, Protein engineering.

The structure of iron superoxide dismutase from Pseudomonas ovalis complexed with the inhibitor azide.

G A Petsko, G. Petsko, B. Stoddard, 1990, Protein engineering.

X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution.

M Karplus, J Kuriyan, G A Petsko, 1986, Journal of molecular biology.

Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant.

G L Kenyon, G A Petsko, G. Petsko, 1995, Biochemistry.

Amino‐aromatic interactions in proteins

G A Petsko, S K Burley, G. Petsko, 1986, FEBS letters.

The role of water in the catalytic efficiency of triosephosphate isomerase.

G A Petsko, G. Petsko, N. Xuong, 1999, Biochemistry.

Structure of yeast triosephosphate isomerase at 1.9-A resolution.

F. C. Hartman, G A Petsko, G. Petsko, 1990, Biochemistry.

26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity.

R L Campbell, G A Petsko, G. Petsko, 1993, Proceedings of the National Academy of Sciences of the United States of America.

The refined crystal structure of subtilisin Carlsberg at 2.5 A resolution.

G A Petsko, G. Petsko, D. Neidhart, 1988, Protein engineering.

Subunit interface of triosephosphate isomerase: site-directed mutagenesis and characterization of the altered enzyme.

G A Petsko, G. Petsko, A. Klibanov, 1987, Biochemistry.

Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop.

M Karplus, G A Petsko, M. Karplus, 1990, Science.

X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.

Karen N. Allen, G A Petsko, G. Petsko, 1994, Biochemistry.

On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase.

D W Banner, G A Petsko, G. Petsko, 1981, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Effect of anisotropy and anharmonicity on protein crystallographic refinement. An evaluation by molecular dynamics.

M Karplus, J Kuriyan, G A Petsko, 1986, Journal of molecular biology.

Use of a minimum perturbation approach to predict TIM mutant structures.

M Karplus, G A Petsko, D Joseph-McCarthy, 1995, Protein engineering.

Study of protein dynamics by X-ray diffraction.

G A Petsko, G. Petsko, D. Ringe, 1986, Methods in enzymology.

Interaction of a peptidomimetic aminimide inhibitor with elastase.

G A Petsko, G. Petsko, D. Ringe, 1995, Science.

Mapping protein dynamics by X-ray diffraction.

G A Petsko, G. Petsko, D. Ringe, 1985, Progress in biophysics and molecular biology.

Structure of oxidized flavodoxin from Anacystis nidulans.

D Tsernoglou, G A Petsko, G. Petsko, 1983, Journal of molecular biology.

Aromatic-aromatic interaction: a mechanism of protein structure stabilization.

G A Petsko, S K Burley, G. Petsko, 1985, Science.

The catalytic pathway of cytochrome p450cam at atomic resolution.

J Berendzen, R M Sweet, D. E. Benson, 2000, Science.

Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.

G A Petsko, G. Petsko, D. Ringe, 1999, Journal of molecular biology.

Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastase.

G A Petsko, G. Petsko, D. Ringe, 1994, Biochemistry.

Structural dynamics of liganded myoglobin.

H Frauenfelder, G A Petsko, G. Petsko, 1980, Biophysical journal.

Design, synthesis, and characterization of a potent xylose isomerase inhibitor, D-threonohydroxamic acid, and high-resolution X-ray crystallographic structure of the enzyme-inhibitor complex.

Karen N. Allen, G A Petsko, G. Petsko, 1995, Biochemistry.

Crystallographic studies of the mechanism of xylose isomerase.

G A Petsko, G. Petsko, D. Ringe, 1989, Biochemistry.

Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway.

M Karplus, G A Petsko, M. Karplus, 1991, Biochemistry.

Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase.

G A Petsko, G. Petsko, D. Ringe, 1999, Biochemistry.

Structure and function of snake venom curarimimetic neurotoxins.

D Tsernoglou, G A Petsko, G. Petsko, 1981, Molecular pharmacology.

The role of mobility in the substrate binding and catalytic machinery of enzymes.

W A Gilbert, G A Petsko, T Alber, 1983, Ciba Foundation symposium.

Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase.

P C Babbitt, G L Kenyon, G A Petsko, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Estimation of uncertainties in X‐ray refinement results by use of perturbed structures

M Karplus, J Kuriyan, G A Petsko, 1987, Proteins.

Structure determination of turkey egg-white lysozyme using Laue diffraction data.

G A Petsko, G. Petsko, J. Hajdu, 1992, Acta crystallographica. Section B, Structural science.

Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins.

G A Petsko, G. Petsko, P. Závodszky, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Chemistry and biology.

G A Petsko, G. Petsko, 2000, Proceedings of the National Academy of Sciences of the United States of America.