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Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics

Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1313184692

Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics

About this item

Full title

Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics

Publisher

United States: Public Library of Science

Journal title

PLoS computational biology, 2011-04, Vol.7 (4), p.e1002034-e1002034

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

Periplasmic binding proteins (PBPs) are a large family of molecular transporters that play a key role in nutrient uptake and chemotaxis in Gram-negative bacteria. All PBPs have characteristic two-domain architecture with a central interdomain ligand-binding cleft. Upon binding to their respective ligands, PBPs undergo a large conformational change...

Alternative Titles

Full title

Accessing a hidden conformation of the maltose binding protein using accelerated molecular dynamics

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_1313184692

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1313184692

Other Identifiers

ISSN

1553-7358,1553-734X

E-ISSN

1553-7358

DOI

10.1371/journal.pcbi.1002034

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