Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected]

RC Milton; SC Milton; SB Kent

doi:10.1126/science.1604320

Article Information

vol. 256 no. 5062 1445-1448

DOI:

https://doi.org/10.1126/science.1604320

PubMed:

1604320

Published By:

American Association for the Advancement of Science

Print ISSN:

0036-8075

Online ISSN:

1095-9203

History:

.

Copyright & Usage:

Author Information

RC Milton,
SC Milton,
SB Kent

Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037.

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View Abstract

Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected]

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Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected]

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Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected]

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Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected]

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Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected]

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