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

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

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 respons...

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Bibliographic Details
Main Authors: Ajda Taler-Verčič, Samra Hasanbašić, Selma Berbić, Veronika Stoka, Dušan Turk, Eva Žerovnik
Format: Article
Language:English
Published: MDPI AG 2017-03-01
Series:International Journal of Molecular Sciences
Subjects:
cis proline
conformational switch
folding intermediate
domain swapping
amyloid fibrils
protein aggregation
stefin B
β2-microglobulin
Online Access:http://www.mdpi.com/1422-0067/18/3/549

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http://www.mdpi.com/1422-0067/18/3/549

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