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Full-Text Articles in Medicine and Health Sciences
The Alphabet Of Intrinsic Disorder: I. Act Like A Pro: On The Abundance And Roles Of Proline Residues In Intrinsically Disordered Proteins, Francois-Xavier Theillet, Lajos Kalmar, Peter Tompa, Kyou-Hoon Han, Philipp Selenko, A. Keith Dunker, Gary W. Daughdrill, Vladimir N. Uversky
The Alphabet Of Intrinsic Disorder: I. Act Like A Pro: On The Abundance And Roles Of Proline Residues In Intrinsically Disordered Proteins, Francois-Xavier Theillet, Lajos Kalmar, Peter Tompa, Kyou-Hoon Han, Philipp Selenko, A. Keith Dunker, Gary W. Daughdrill, Vladimir N. Uversky
Molecular Medicine Faculty Publications
A significant fraction of every proteome is occupied by biologically active proteins that do not form unique three-dimensional structures. These intrinsically disordered proteins (IDPs) and IDP regions (IDPRs) have essential biological functions and are characterized by extensive structural plasticity. Such structural and functional behavior is encoded in the amino acid sequences of IDPs/IDPRs, which are enriched in disorder-promoting residues and depleted in order-promoting residues. In fact, amino acid residues can be arranged according to their disorder-promoting tendency to form an alphabet of intrinsic disorder that defines the structural complexity and diversity of IDPs/IDPRs. This review is the first in a …
The Alphabet Of Intrinsic Disorder: Ii. Various Roles Of Glutamic Acid In Ordered And Intrinsically Disordered Proteins, Vladimir N. Uversky
The Alphabet Of Intrinsic Disorder: Ii. Various Roles Of Glutamic Acid In Ordered And Intrinsically Disordered Proteins, Vladimir N. Uversky
Molecular Medicine Faculty Publications
The ability of a protein to fold into unique functional state or to stay intrinsically disordered is encoded in its amino acid sequence. Both ordered and intrinsically disordered proteins (IDPs) are natural polypeptides that use the same arsenal of 20 proteinogenic amino acid residues as their major building blocks. The exceptional structural plasticity of IDPs, their capability to exist as heterogeneous structural ensembles and their wide array of important disorder-based biological functions that complements functional repertoire of ordered proteins are all rooted within the peculiar differential usage of these building blocks by ordered proteins and IDPs. In fact, some residues …
Biophysical Characterization Of Α-Synuclein And Rotenone Interaction, Blanca A. Silva, Olöf Einarsdóttir, Anthony L. Fink, Vladimir N. Uversky
Biophysical Characterization Of Α-Synuclein And Rotenone Interaction, Blanca A. Silva, Olöf Einarsdóttir, Anthony L. Fink, Vladimir N. Uversky
Molecular Medicine Faculty Publications
Previous studies revealed that pesticides interact with α-synuclein and accelerate the rate of fibrillation. These results are consistent with the prevailing hypothesis that the direct interaction of α-synuclein with pesticides is one of many suspected factors leading to α-synuclein fibrillation and ultimately to Parkinson's disease. In this study, the biophysical properties and fibrillation kinetics of α-synuclein in the presence of rotenone were investigated and, more specifically, the effects of rotenone on the early-stage misfolded forms of α-synuclein were considered. The thioflavine T (ThT) fluorescence assay studies provide evidence that early-phase misfolded α-synuclein forms are affected by rotenone and that the …