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Article

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

1
Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia
2
CIPKeBiP—Center of Excellence for Integrated Approaches in Chemistry and Biology of Proteins, Jamova 39, 1000 Ljubljana, Slovenia
3
Jožef Stefan International Postgraduate School, Jamova 39, 1000 Ljubljana, Slovenia
4
Faculty of Pharmacy, Department of Biochemistry, University of Tuzla, Univerzitetska 1, 75000 Tuzla, Bosnia and Herzegovina
*
Author to whom correspondence should be addressed.
Academic Editor: Salvador Ventura
Int. J. Mol. Sci. 2017, 18(3), 549; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms18030549
Received: 11 January 2017 / Revised: 20 February 2017 / Accepted: 23 February 2017 / Published: 7 March 2017
(This article belongs to the Collection Protein Folding)
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 findings are compared to β2-microglobulin, a protein involved in dialysis-related amyloidosis. The assessment of the contribution of proline residues to the process of amyloid fibril formation may shed new light on the critical molecular events involved in conformational disorders. View Full-Text
Keywords: cis proline; conformational switch; folding intermediate; domain swapping; amyloid fibrils; protein aggregation; stefin B; β2-microglobulin cis proline; conformational switch; folding intermediate; domain swapping; amyloid fibrils; protein aggregation; stefin B; β2-microglobulin
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MDPI and ACS Style

Taler-Verčič, A.; Hasanbašić, S.; Berbić, S.; Stoka, V.; Turk, D.; Žerovnik, E. Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation. Int. J. Mol. Sci. 2017, 18, 549. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms18030549

AMA Style

Taler-Verčič A, Hasanbašić S, Berbić S, Stoka V, Turk D, Žerovnik E. Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation. International Journal of Molecular Sciences. 2017; 18(3):549. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms18030549

Chicago/Turabian Style

Taler-Verčič, Ajda, Samra Hasanbašić, Selma Berbić, Veronika Stoka, Dušan Turk, and Eva Žerovnik. 2017. "Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation" International Journal of Molecular Sciences 18, no. 3: 549. https://0-doi-org.brum.beds.ac.uk/10.3390/ijms18030549

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