Log in to save to my catalogue

Evolution of tunnels in α/β-hydrolase fold proteins-What can we learn from studying epoxide hydrolas...

Evolution of tunnels in α/β-hydrolase fold proteins-What can we learn from studying epoxide hydrolas...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2677645494

Evolution of tunnels in α/β-hydrolase fold proteins-What can we learn from studying epoxide hydrolases?

About this item

Full title

Evolution of tunnels in α/β-hydrolase fold proteins-What can we learn from studying epoxide hydrolases?

Publisher

United States: Public Library of Science

Journal title

PLoS computational biology, 2022-05, Vol.18 (5), p.e1010119-e1010119

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

The evolutionary variability of a protein's residues is highly dependent on protein region and function. Solvent-exposed residues, excluding those at interaction interfaces, are more variable than buried residues whereas active site residues are considered to be conserved. The abovementioned rules apply also to α/β-hydrolase fold proteins-one of th...

Alternative Titles

Full title

Evolution of tunnels in α/β-hydrolase fold proteins-What can we learn from studying epoxide hydrolases?

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_2677645494

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2677645494

Other Identifiers

ISSN

1553-7358,1553-734X

E-ISSN

1553-7358

DOI

10.1371/journal.pcbi.1010119

How to access this item