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Illuminating the mechanistic roles of enzyme conformational dynamics

Illuminating the mechanistic roles of enzyme conformational dynamics

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_osti_scitechconnect_1001563

Illuminating the mechanistic roles of enzyme conformational dynamics

About this item

Full title

Illuminating the mechanistic roles of enzyme conformational dynamics

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2007-11, Vol.104 (46), p.18055-18060

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Many enzymes mold their structures to enclose substrates in their active sites such that conformational remodeling may be required during each catalytic cycle. In adenylate kinase (AK), this involves a large-amplitude rearrangement of the enzyme's lid domain. Using our method of high-resolution single-molecule FRET, we directly followed AK's domain...

Alternative Titles

Full title

Illuminating the mechanistic roles of enzyme conformational dynamics

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_osti_scitechconnect_1001563

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_osti_scitechconnect_1001563

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0708600104

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