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Article

Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation.

International journal of molecular sciences - 7 Mar 2017

Taler-Verčič Ajda, Hasanbašić Samra, Berbić Selma, Stoka Veronika, Turk Dušan, Žerovnik Eva

Abstract excerpt

Here we discuss studies of the structure, folding, oligomerization and amyloid fibril formation of several proline mutants of human stefin B, which is a protein inhibitor of lysosomal cysteine cathepsins and a member of the cystatin family. The structurally important prolines in stefin B are responsible for the slow folding phases and facilitate domain swapping (Pro 74) and loop swapping (Pro 79). Moreover, our...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 28272335
DOI: 10.3390/ijms18030549
PMCID: PMC5372565

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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