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Presents novel information which cannot be found in other textbooks and monographs
Provides one of the most up to date presentations of current biophysics
The first book to cover all of the 10 currently most important biophysical methods
Details exciting recent discoveries and developments in the fields of biophysical nanotechnology, scanning probe microscopy, ion mobility spectrometry, mass spectrometry and proteomics
Introduces rapid partial protein ladder sequencing - an important method for fast and highly sensitive identification of proteins
Describes the determination of interaction surfaces in protein complexes by mass spectrometric mapping of binding of chemical linkers - a method to support the high-resolution structural analysis of large macromolecular assemblies
Over 250 figures support a quick understanding of technological details, plus worked examples in the text and solutions to problems facilitate teaching
Incorporating recent dramatic advances, this textbook presents a fresh and timely introduction to modern biophysical methods. An array of new, faster and higher-power biophysical methods now enables scientists to examine the mysteries of life at a molecular level. This innovative text surveys and explains the ten key biophysical methods, including those related to biophysical nanotechnology, scanning probe microscopy, X-ray crystallography, ion mobility spectrometry, mass spectrometry, proteomics, and protein folding and structure. Incorporating much information previously unavailable in tutorial form, Nölting employs worked examples and about 270 illustrations to fully detail the techniques and their underlying mechanisms. Methods in Modern Biophysics is written for advanced undergraduate and graduate students, postdocs, researchers, lecturers, and professors in biophysics, biochemistry and related fields.
Special features in the 3rd edition: Introduces rapid partial protein ladder sequencing - an important method for fast and highly sensitive identification of proteins, describes the determination of interaction surfaces in protein complexes by mass spectrometric mapping of binding of chemical linkers - a method to support the high-resolution structural analysis of large macromolecular assemblies.