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References from COMPUTATIONAL ENZYME DESIGN: ADVANCES, HURDLES AND POSSIBLE WAYS FORWARD. Local targets link to admitted publications; unresolved targets remain external evidence.
Unresolved reference
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A generic program for multistate protein design
10.1371/journal.pone.0020937 · 2011 · External reference
Rosetta re-model: A generalized framework for flexible backbone protein design
10.1371/journal.pone.0024109 · 2011 · External reference
Unresolved reference
External reference
10.1038/nature09304
10.1038/nature09304 · External reference
Crystal structure of a monomeric retroviral protease solved by protein folding game players
10.1038/nsmb.2119 · 2011 · External reference
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10.1002/pro.481
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10.1093/protein/gzr006
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The depth of chemical time and the power of enzymes as catalysts
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Flexibility, diversity, and cooperativity: Pillars of enzyme catalysis
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Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites
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Enzyme-like proteins by computational design
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10.1126/science.1098432 · External reference
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De novo enzyme design using rosetta3
10.1371/journal.pone.0019230 · 2011 · External reference
10.1073/pnas.97.19.10383
10.1073/pnas.97.19.10383 · External reference
10.1016/s1367-5931(98)80112-9
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Challenges and advances in validating enzyme design proposals: The case of kemp eliminase catalysis
10.1021/bi200063a · 2011 · External reference
10.1016/j.jmb.2011.01.041
10.1016/j.jmb.2011.01.041 · External reference
Molecular architecture and biological reactions
10.1021/cen-v024n010.p1375 · 1946 · External reference
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10.1038/161707a0 · 1948 · External reference
10.1021/jp953748q
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10.1007/978-1-4684-9978-0_2
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10.1126/science.7809611
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A view at the millennium: the efficiency of enzymatic catalysis
10.1021/ar0001665 · 2002 · External reference
10.1126/science.1085515
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Energetics of enzyme catalysis
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Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
10.1073/pnas.68.8.1678 · 1971 · External reference
Alternative view of enzyme reactions
10.1073/pnas.82.8.2225 · 1985 · External reference
Testing electrostatic complementarity in enzyme catalysis: Hydrogen bonding in the ketosteroid isomerase oxyanion hole
10.1371/journal.pbio.0040099 · 2006 · External reference
10.1073/pnas.1111252108
10.1073/pnas.1111252108 · External reference
The near attack conformation approach to the study of the chorismate to prephenate reaction
10.1073/pnas.1534873100 · 2003 · External reference
Apparent nac effect in chorismate mutase reflects electrostatic transition state stabilization
10.1021/ja0356481 · 2003 · External reference
A new perspective on chemical and physical processes: the reaction force
10.1080/00268970701604663 · 2007 · External reference
How an enzyme surmounts the activation energy barrier
10.1073/pnas.2235806100 · 2003 · External reference
10.1021/ja905396s
10.1021/ja905396s · External reference
10.1073/pnas.0913638107
10.1073/pnas.0913638107 · External reference
Exploring challenges in rational enzyme design by simulating the catalysis in artificial kemp eliminase
10.1073/pnas.1010381107 · 2010 · External reference
10.1002/pro.462
10.1002/pro.462 · External reference
10.1021/jo901503d
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10.1002/1439-7633(20011203)2:12<873::aid-cbic873>3.0.co;2-a
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10.1039/b814552k
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10.1021/ja043905b
10.1021/ja043905b · External reference
10.1007/s00894-010-0775-8
10.1007/s00894-010-0775-8 · External reference
Enzyme promiscuity: mechanism and applications
10.1016/j.tibtech.2007.03.002 · 2007 · External reference
10.1016/s1367-5931(98)80091-4
10.1016/s1367-5931(98)80091-4 · External reference
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10.1016/s1074-5521(99)80033-7 · External reference
10.1021/ci200177d
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10.1002/pro.2055
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10.1073/pnas.1118082108
10.1073/pnas.1118082108 · External reference
10.1021/bi802191b
10.1021/bi802191b · External reference
Ground state and transition state contributions to the rates of intramolecular and enzymatic reactions
10.1021/ar960131y · 1999 · External reference
Recent developments of the quantum chemical cluster approach for modeling enzyme reactions
10.1007/s00775-009-0511-y · 2009 · External reference
10.1038/nbt.2109
10.1038/nbt.2109 · External reference
10.1021/cr0503106
10.1021/cr0503106 · External reference
10.1039/c2cc31502e
10.1039/c2cc31502e · External reference
