Intrinsically Disordered Proteins Structural (14 results)

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Buch. Condition: Neu. Neuware - Intrinsically disordered proteins (IDPs) are biomolecules that do not have a definite 3D structure; their role in the biochemical network of a cell relates to their ability to switch rapidly among different secondary and tertiary structures. The emergence of IDPs has challenged the classical protein structure-function paradigm. IDPs play an important role in cellular regulation, signaling and control in health and disease. However, the unusual biophysics of these proteins makes structural characterisation of IDPs and their complexes not only challenging but often resulting in opposite conclusions. This book studies the structural characterisation and future directions of IDPs. Chapter One focuses on the DNA-binding IDPs and how intrinsic disorder affects their function. Chapter Two discusses the use of a computer atomistic simulation for the structural analysis of IDPs. The final chapter, Chapter Three, examines two long-standing contradictions concerning dimerisation and membrane-binding activities of IDPs; provides an explanation of these discrepancies; and demonstrates how the resolution of these critical issues in the field results in the expanded understanding of cell function with multiple applications in biology and medicine.…

Condition: New. Editor(s): Weber, Violet. Num Pages: 120 pages. BIC Classification: PSBC. Category: (P) Professional & Vocational. Dimension: 162 x 239 x 13. Weight in Grams: 322. . 2016. UK ed. Hardcover. . . . . Books ship from the US and Ireland.

Condition: New. Editor(s): Weber, Violet. Num Pages: 120 pages. BIC Classification: PSBC. Category: (P) Professional & Vocational. Dimension: 162 x 239 x 13. Weight in Grams: 322. . 2016. UK ed. Hardcover. . . . .

Taschenbuch. Condition: Neu. Structural dynamics of intrinsically disordered proteins | The UmuD proteins are molecular adaptors in the regulation of DNA damage tolerance | Jaylene Ollivierre | Taschenbuch | 168 S. | Englisch | 2013 | LAP LAMBERT Academic Publishing | EAN 9783659326066 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.…

Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -The homodimeric umuD gene products play key roles in regulating the cellular response to DNA damage in Escherichia coli. UmuD2 is composed of 139-amino acid subunits and is upregulated as part of the SOS DNA damage response. Subsequently, damage-induced RecA:ssDNA nucleoprotein filaments mediate the slow autocleavage of the N-terminal 24-amino acid arms of UmuD2 yielding UmuD'2. It was previously proposed that UmuD cleaves only in the trans conformation, in which the arm of one monomer utilizes that active site of the adjacent monomer for cleavage. Cleavage in trans would therefore require dimerization. However, isoenergetic models of UmuD2 suggested that the arms may adopt cis (intramolecular) or trans (intermolecular) conformations, and may be unbound from or bound to the globular C-terminal domain. The dynamic nature of the N-terminal arms may explain how a number of distinct protein-protein contacts that prevent and facilitate mutagenic translesion synthesis (TLS) are made. Here we discuss how the conformation and dynamics of the UmuD proteins regulate the DNA damage response. 168 pp. Englisch.…

Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - The homodimeric umuD gene products play key roles in regulating the cellular response to DNA damage in Escherichia coli. UmuD2 is composed of 139-amino acid subunits and is upregulated as part of the SOS DNA damage response. Subsequently, damage-induced RecA:ssDNA nucleoprotein filaments mediate the slow autocleavage of the N-terminal 24-amino acid arms of UmuD2 yielding UmuD'2. It was previously proposed that UmuD cleaves only in the trans conformation, in which the arm of one monomer utilizes that active site of the adjacent monomer for cleavage. Cleavage in trans would therefore require dimerization. However, isoenergetic models of UmuD2 suggested that the arms may adopt cis (intramolecular) or trans (intermolecular) conformations, and may be unbound from or bound to the globular C-terminal domain. The dynamic nature of the N-terminal arms may explain how a number of distinct protein-protein contacts that prevent and facilitate mutagenic translesion synthesis (TLS) are made. Here we discuss how the conformation and dynamics of the UmuD proteins regulate the DNA damage response.…

Condition: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Ollivierre JayleneJaylene Ollivierre, PhD: Studied Biological Chemistry at Northeastern University. Postdoctoral researcher at MIT, Boston.The homodimeric umuD gene products play key roles in regulating the cellular response to .…

Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -The homodimeric umuD gene products play key roles in regulating the cellular response to DNA damage in Escherichia coli. UmuD2 is composed of 139-amino acid subunits and is upregulated as part of the SOS DNA damage response. Subsequently, damage-induced RecA:ssDNA nucleoprotein filaments mediate the slow autocleavage of the N-terminal 24-amino acid arms of UmuD2 yielding UmuD¿2. It was previously proposed that UmuD cleaves only in the trans conformation, in which the arm of one monomer utilizes that active site of the adjacent monomer for cleavage. Cleavage in trans would therefore require dimerization. However, isoenergetic models of UmuD2 suggested that the arms may adopt cis (intramolecular) or trans (intermolecular) conformations, and may be unbound from or bound to the globular C-terminal domain. The dynamic nature of the N-terminal arms may explain how a number of distinct protein-protein contacts that prevent and facilitate mutagenic translesion synthesis (TLS) are made. Here we discuss how the conformation and dynamics of the UmuD proteins regulate the DNA damage response.OmniScriptum SRL, Str. Armeneasca 28/1, office 1, 2012 Chisinau 168 pp. Englisch.…