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Peter Schuck

Researcher at National Institutes of Health

Publications -  256
Citations -  21407

Peter Schuck is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Sedimentation coefficient & Analytical Ultracentrifugation. The author has an hindex of 66, co-authored 248 publications receiving 19643 citations. Previous affiliations of Peter Schuck include Goethe University Frankfurt & University of Connecticut.

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Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

TL;DR: A new method for the size-distribution analysis of polymers by sedimentation velocity analytical ultracentrifugation that exploits the ability of Lamm equation modeling to discriminate between the spreading of the sedimentation boundary arising from sample heterogeneity and from diffusion is described.
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Grafting of “Abbreviated” Complementarity-Determining Regions Containing Specificity-Determining Residues Essential for Ligand Contact to Engineer a Less Immunogenic Humanized Monoclonal Antibody

TL;DR: The final variant of the HuCOL-1, which retains its Ag-binding reactivity and shows significantly lower serum reactivity than that of the parental Ab, can serve as a prototype for the development of a potentially useful clinical reagent.
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Modern analytical ultracentrifugation in protein science: A tutorial review

TL;DR: Sedimentation equilibrium of proteins, including membrane proteins and glycoproteins, is the method of choice for molar mass determinations and the study of self‐association and heterogeneous interactions, such as protein–protein, protein–nucleic acid, and protein–small molecule binding.
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Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems.

TL;DR: It is shown that the least-squares approach ls-g*(s) can be extrapolated to infinite time by considering area divisions analogous to boundary divisions in the van Holde-Weischet method, thus allowing the transformation of interference optical data into an integral sedimentation coefficient distribution G(s).
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Use of surface plasmon resonance to probe the equilibrium and dynamic aspects of interactions between biological macromolecules.

TL;DR: The use of surface plasmon resonance biosensors to measure the binding affinities and the kinetic constants of reversible interactions between biological macromolecules is reviewed.