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Atomic view of the histidine environment stabilizing higher-pH conformations of pH-dependent protein...

Atomic view of the histidine environment stabilizing higher-pH conformations of pH-dependent protein...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4518280

Atomic view of the histidine environment stabilizing higher-pH conformations of pH-dependent proteins

About this item

Full title

Atomic view of the histidine environment stabilizing higher-pH conformations of pH-dependent proteins

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2015-07, Vol.6 (1), p.7771-7771, Article 7771

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

External stimuli are powerful tools that naturally control protein assemblies and functions. For example, during viral entry and exit changes in pH are known to trigger large protein conformational changes. However, the molecular features stabilizing the higher pH structures remain unclear. Here we elucidate the conformational change of a self-asse...

Alternative Titles

Full title

Atomic view of the histidine environment stabilizing higher-pH conformations of pH-dependent proteins

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4518280

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4518280

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms8771

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