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Delicate balance among thermal stability, binding affinity, and conformational space explored by sin...

Delicate balance among thermal stability, binding affinity, and conformational space explored by sin...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_94c6e8e43a92458194b1a6a09e1f51ed

Delicate balance among thermal stability, binding affinity, and conformational space explored by single-domain VHH antibodies

About this item

Full title

Delicate balance among thermal stability, binding affinity, and conformational space explored by single-domain VHH antibodies

Publisher

London: Nature Publishing Group UK

Journal title

Scientific reports, 2021-10, Vol.11 (1), p.20624-9, Article 20624

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The high binding affinities and specificities of antibodies have led to their use as drugs and biosensors. Single-domain V
H
H antibodies exhibit high specificity and affinity but have higher stability and solubility than conventional antibodies as they are single-domain proteins. In this work, based on physicochemical measurements and molecu...

Alternative Titles

Full title

Delicate balance among thermal stability, binding affinity, and conformational space explored by single-domain VHH antibodies

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_94c6e8e43a92458194b1a6a09e1f51ed

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_94c6e8e43a92458194b1a6a09e1f51ed

Other Identifiers

ISSN

2045-2322

E-ISSN

2045-2322

DOI

10.1038/s41598-021-98977-8

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