Glycation induced conformational alterations in caprine brain cystatin (CBC) leads to aggregation via passage through a partially folded state

2018 ◽  
Vol 106 ◽  
pp. 917-929 ◽  
Author(s):  
Peerzada Shariq Shaheen Khaki ◽  
Anna Feroz ◽  
Azad Alam Siddiqui ◽  
Syed Mudasir Qadri ◽  
Fakhra Amin ◽  
...  
Keyword(s):  
Partially Folded State

Backbone Dynamics of Apocytochromeb5in Its Native, Partially Folded State†

Biochemistry ◽  
1999 ◽  
Vol 38 (8) ◽  
pp. 2577-2589 ◽  
Author(s):  
Shibani Bhattacharya ◽  
Christopher J. Falzone ◽  
Juliette T. J. Lecomte
Keyword(s):  
Backbone Dynamics ◽  
Partially Folded State

scholarly journals Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity

2018 ◽  
Vol 293 (26) ◽  
pp. 10303-10313 ◽  
Author(s):  
Edoardo Del Poggetto ◽  
Angelo Toto ◽  
Chiara Aloise ◽  
Francesco Di Piro ◽  
Ludovica Gori ◽  
...  
Keyword(s):  
Aggregation Propensity ◽  
Partially Folded State

Conformational Switch upon Phosphorylation: Human CDK Inhibitor p19INK4d between the Native and Partially Folded State

2008 ◽  
Vol 4 (1) ◽  
pp. 53-63 ◽  
Author(s):  
Christian Löw ◽  
Nadine Homeyer ◽  
Ulrich Weininger ◽  
Heinrich Sticht ◽  
Jochen Balbach
Keyword(s):  
Cdk Inhibitor ◽  
Conformational Switch ◽  
Partially Folded State

Characterization of a Trifluoroethanol-induced Partially Folded State of α-Lactalbumin

1994 ◽  
Vol 235 (2) ◽  
pp. 587-599 ◽  
Author(s):  
Andrei T. Alexandrescu ◽  
Yuet-Lan Ng ◽  
Christopher M. Dobson
Keyword(s):  
Partially Folded State

Native-like β-structure in a Trifluoroethanol-induced Partially Folded State of the All-β-sheet Protein Tendamistat

1996 ◽  
Vol 260 (3) ◽  
pp. 432-445 ◽  
Author(s):  
Nancy Schönbrunner ◽  
Josef Wey ◽  
Joachim Engels ◽  
Holger Georg ◽  
Thomas Kiefhaber
Keyword(s):  
Partially Folded State ◽  
Β Sheet

scholarly journals A Glimpse into the Structural Properties of the Intermediate and Transition State in the Folding of Bromodomain 2 Domain 2 by Φ Value Analysis

2021 ◽  
Vol 22 (11) ◽  
pp. 5953
Author(s):  
Leonore Novak ◽  
Maria Petrosino ◽  
Daniele Santorelli ◽  
Roberta Chiaraluce ◽  
Valerio Consalvi ◽  
...  
Keyword(s):  
Transition State ◽  
Chromatin Remodeling ◽  
Mutational Analysis ◽  
Structural Information ◽  
Terminal Region ◽  
Folding Pathway ◽  
Value Analysis ◽  
Folding Nucleus ◽  
Late Transition ◽  
Partially Folded State

Bromodomains (BRDs) are small protein interaction modules of about 110 amino acids that selectively recognize acetylated lysine in histones and other proteins. These domains have been identified in a variety of multi-domain proteins involved in transcriptional regulation or chromatin remodeling in eukaryotic cells. BRD inhibition is considered an attractive therapeutic approach in epigenetic disorders, particularly in oncology. Here, we present a Φ value analysis to investigate the folding pathway of the second domain of BRD2 (BRD2(2)). Using an extensive mutational analysis based on 25 site-directed mutants, we provide structural information on both the intermediate and late transition state of BRD2(2). The data reveal that the C-terminal region represents part of the initial folding nucleus, while the N-terminal region of the domain consolidates its structure only later in the folding process. Furthermore, only a small number of native-like interactions have been identified, suggesting the presence of a non-compact, partially folded state with scarce native-like characteristics. Taken together, these results indicate that, in BRD2(2), a hierarchical mechanism of protein folding can be described with non-native interactions that play a significant role in folding.

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