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Article

Amyloid fibril formation by circularly permuted and C-terminally deleted mutants.

International journal of biological macromolecules - 1 May 2011

Corrêa Daniel H A, Ramos Carlos H I

Abstract excerpt

The natural N- and C-termini, i.e., the given order of secondary structure segments, are critical for protein folding and stability, as shown by several studies using circularly permuted proteins, mutants that have their N- and C-termini linked and are then digested at another site to create new termini. A previous work showed that circularly permuted mutants of sperm whale myoglobin (Mb) are functional, have...

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Identifiers

PMID: 21300089
DOI: 10.1016/j.ijbiomac.2011.01.027

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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