Local Structural Preferences of Calpastatin, the Intrinsically Unstructured Protein Inhibitor of Calpain†‡§

Biochemistry ◽  
2008 ◽  
Vol 47 (26) ◽  
pp. 6936-6945 ◽  
Author(s):  
Robert Kiss ◽  
Dénes Kovács ◽  
Péter Tompa ◽  
András Perczel
Keyword(s):  
Protein Inhibitor ◽  
Intrinsically Unstructured Protein ◽  
Structural Preferences ◽  
Unstructured Protein

BQP35 is a novel member of the intrinsically unstructured protein (IUP) family which is a potential antigen for the sero-diagnosis of Babesia sp. BQ1 (Lintan) infection

2012 ◽  
Vol 187 (3-4) ◽  
pp. 421-430 ◽  
Author(s):  
Guiquan Guan ◽  
Emmanuelle Moreau ◽  
Junlong Liu ◽  
Miling Ma ◽  
Hélène Rogniaux ◽  
...  
Keyword(s):  
Intrinsically Unstructured Protein ◽  
Unstructured Protein

scholarly journals Alpha-Synuclein, an Intrinsically Unstructured Protein. How Interesting Can It Be?

2013 ◽  
Vol 104 (2) ◽  
pp. 5a
Author(s):  
Alexander Maltsev ◽  
Jinfa Ying ◽  
Yang Shen ◽  
Ad Bax
Keyword(s):  
Alpha Synuclein ◽  
Intrinsically Unstructured Protein ◽  
Unstructured Protein

Human Regulatory Protein Ki-1/57 Has Characteristics of an Intrinsically Unstructured Protein

2008 ◽  
Vol 7 (10) ◽  
pp. 4465-4474 ◽  
Author(s):  
Gustavo C. Bressan ◽  
Júlio C. Silva ◽  
Júlio C. Borges ◽  
Dario O. dos Passos ◽  
Carlos H. I. Ramos ◽  
...  
Keyword(s):  
Regulatory Protein ◽  
Intrinsically Unstructured Protein ◽  
Unstructured Protein

MpAsr encodes an intrinsically unstructured protein and enhances osmotic tolerance in transgenic Arabidopsis

2011 ◽  
Vol 30 (7) ◽  
pp. 1219-1230 ◽  
Author(s):  
Jin-Ran Dai ◽  
Bing Liu ◽  
Dong-Ru Feng ◽  
Hai-yan Liu ◽  
Yan-ming He ◽  
...  
Keyword(s):  
Transgenic Arabidopsis ◽  
Osmotic Tolerance ◽  
Intrinsically Unstructured Protein ◽  
Unstructured Protein

Structure and dynamics changes induced by 2,2,2-trifluoro-ethanol (TFE) on the N-terminal half of hepatitis C virus core proteinThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

2010 ◽  
Vol 88 (2) ◽  
pp. 315-323 ◽  
Author(s):  
Jean-Baptiste Duvignaud ◽  
Denis Leclerc ◽  
Stéphane M. Gagné
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Core Protein ◽  
Peer Review Process ◽  
Helical Structure ◽  
Functional Roles ◽  
Virus Core ◽  
Hcv Core Protein ◽  
Intrinsically Unstructured Protein ◽  
Unstructured Protein

The Core protein of hepatitis C virus is involved in several interactions other than the encapsidation of viral RNA. We recently proposed that this is related to the fact that the N-terminal half of this protein (C82) is an intrinsically unstructured protein (IUP) domain. IUP domains can adopt a secondary structure when they are interacting with another molecule, such as a nucleic acid or a protein. It is also possible to mimic these conditions by modifying the environment of the protein. We investigated the propensity of this protein to fold as a function of salt concentration, detergent, pH, and 2,2,2-trifluoro-ethanol (TFE); only the addition of TFE resulted in a structural change. The effect of TFE addition was studied by circular dichroism, structural, and dynamic data obtained by NMR. The data indicate that C82 can adopt an α-helical structure; this conformation is likely relevant to one of the functional roles of the HCV Core protein.

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