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Structural Analysis of Hen Egg Lysozyme Refolded after Denaturation at Acidic pH

Structural Analysis of Hen Egg Lysozyme Refolded after Denaturation at Acidic pH

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_2624199987

Structural Analysis of Hen Egg Lysozyme Refolded after Denaturation at Acidic pH

About this item

Full title

Structural Analysis of Hen Egg Lysozyme Refolded after Denaturation at Acidic pH

Publisher

New York: Springer US

Journal title

The Protein Journal, 2022-02, Vol.41 (1), p.71-78

Language

English

Formats

Publication information

Publisher

New York: Springer US

More information

Scope and Contents

Contents

Protein structures fluctuate in solution; therefore, proteins have multiple stable structures that are slightly different from each other. In this study, we determined the crystal structure of hen egg lysozyme refolded after denaturation at acidic pH (rHEL) and found a structure different from native HEL (nHEL). The different local conformations of...

Alternative Titles

Full title

Structural Analysis of Hen Egg Lysozyme Refolded after Denaturation at Acidic pH

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_2624199987

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_2624199987

Other Identifiers

ISSN

1572-3887

E-ISSN

1573-4943,1875-8355

DOI

10.1007/s10930-021-10036-3

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