Intrinsically disordered proteins dynamics (19 Ergebnisse)

Zustand: As New. Unread book in perfect condition.

Zustand: New.

Zustand: New.

Zustand: As New. Unread book in perfect condition.

Zustand: New.

Zustand: New. 2019. 1st Edition. paperback. . . . . .

Hardcover. Zustand: Brand New. 254 pages. 11.00x8.50x11.00 inches. In Stock.

Kartoniert / Broschiert. Zustand: New. Provides in-depth discussion of fundamental IDP and IDR dynamics, function, and binding, with mechanistic insight to support new drug development Describes the role of new computational and experimental approaches in characterizing the bin.

Paperback. Zustand: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.

Buch. Zustand: Neu. Neuware - Intrinsically disordered proteins (IDPs) are a class of proteins that do not fold into a specific three-dimensional structure, which is a characteristic of proteins. The structural flexibility of IDPs range from fully structured to partially structured, which enables them to complement ordered proteins in order to perform functions that cannot be performed by rigid structures. Several factors such as pH and temperature can affect the shape and level of disorder in proteins. IDPs have been associated with various diseases such as cancer and cardiovascular diseases. The accumulation of an IDP called a-synuclein plays a pathophysiological role in Parkinson's disease (PD). The structural flexibility of the unstructured a-synuclein protein and associated disease mechanisms is affected by several factors such as genetics, oxidative stress, nitrative stress, and mitochondrial impairment. The book aims to shed light on some of the unexplored aspects of intrinsically disordered proteins and the recent researches on them. It will serve as a valuable source of reference for the graduate and postgraduate students.…

Paperback. Zustand: Brand New. 328 pages. 9.25x7.50x0.71 inches. In Stock.

Zustand: New. 2019. 1st Edition. paperback. . . . . . Books ship from the US and Ireland.

Paperback / softback. Zustand: New. New copy - Usually dispatched within 4 working days.

Taschenbuch. Zustand: 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. Zustand: 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. Zustand: 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.…

Zustand: 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 .…

Hardback. Zustand: New. This item is printed on demand. New copy - Usually dispatched within 5-9 working days.

Taschenbuch. Zustand: 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.…