Buch, Englisch, Band 337, 212 Seiten, Format (B × H): 160 mm x 241 mm, Gewicht: 4616 g
Reihe: Topics in Current Chemistry
Buch, Englisch, Band 337, 212 Seiten, Format (B × H): 160 mm x 241 mm, Gewicht: 4616 g
Reihe: Topics in Current Chemistry
ISBN: 978-3-642-38961-0
Verlag: Springer
Christopher M. Cheatum and Amnon Kohen, Relationship of Femtosecond–Picosecond Dynamics to Enzyme-Catalyzed H-Transfer. Cindy Schulenburg and Donald Hilvert, Protein Conformational Disorder and Enzyme Catalysis. A. Joshua Wand, Veronica R. Moorman and Kyle W. Harpole,
A Surprising Role for Conformational Entropy in Protein Function. Travis P. Schrank, James O. Wrabl and Vincent J. Hilser, Conformational Heterogeneity Within the LID Domain Mediates Substrate Binding to Escherichia coli Adenylate Kinase: Function Follows Fluctuations. Buyong Ma and Ruth Nussinov,
Structured Crowding and Its Effects on Enzyme Catalysis. Michael D. Daily, Haibo Yu, George N. Phillips Jr and Qiang Cui, Allosteric Activation Transitions in Enzymes and Biomolecular Motors: Insights from Atomistic and Coarse-Grained Simulations. Karunesh Arora and Charles L. Brooks III, Multiple Intermediates, Diverse Conformations, and Cooperative Conformational Changes Underlie the Catalytic Hydride Transfer Reaction of Dihydrofolate Reductase. Steven D. Schwartz, Protein Dynamics and the Enzymatic Reaction Coordinate.
Zielgruppe
Research
Autoren/Hrsg.
Weitere Infos & Material
Relationship of Femtosecond–Picosecond Dynamics to Enzyme-Catalyzed H-Transfer.- Protein Conformational Disorder and Enzyme Catalysis.- A Surprising Role for Conformational Entropy in Protein Function.- Conformational Heterogeneity Within the LID Domain Mediates Substrate Binding to Escherichia coli Adenylate Kinase: Function Follows Fluctuations.- Structured Crowding and Its Effects on Enzyme Catalysis.- Allosteric Activation Transitions in Enzymes and Biomolecular Motors: Insights from Atomistic and Coarse-Grained Simulations.- Multiple Intermediates, Diverse Conformations, and Cooperative Conformational Changes Underlie the Catalytic Hydride Transfer Reaction of Dihydrofolate Reductase.- Protein Dynamics and the Enzymatic Reaction Coordinate.
