By Igor A. Kaltashov
"Recent advances in mass spectrometry (MS) have driven the frontiers of analytical chemistry into the biophysical laboratory. for that reason, the biophysical community's recognition of MS-based tools, used to review protein higher-order constitution and dynamics, has speeded up the growth of biophysical MS." "Despite this becoming development, before no unmarried textual content has provided the whole array of MS-based experimental options and techniques for biophysics. Mass Spectrometry in Biophysics expertly closes this hole within the literature."."Covering the theoretical heritage and technical facets of every procedure, this much-needed reference deals an remarkable evaluate of the present kingdom of biophysical MS. Mass Spectrometry in Biophysics starts off with a worthwhile dialogue of basic biophysical strategies and MS-related techniques." "Fully referenced and containing a useful appendix at the physics of electrospray mass spectrometry, Mass Spectrometry in Biophysics additionally bargains a compelling examine the present demanding situations dealing with biomolecular MS and the aptitude purposes that may most likely form its future."--BOOK JACKET. learn more... content material: common evaluation of easy thoughts in molecular biophysics. -- assessment of "traditional" experimental arsenal to review biomolecular constitution and dynamics. -- evaluation of organic mass spectrometry. -- Mass spectrometry-based ways to review biomolecular higher-order constitution. -- Mass spectrometry-based methods to review biomolecular dynamics equilibrium intermediates. -- Kinetic stories by way of mass spectrometry. -- Protein interplay: a more in-depth examine "structure-dynamics-function" triad. -- Synergism among biophysical concepts. -- different biopolymers and artificial polymers of organic curiosity. -- Biomolecular ions in a solvent-free surroundings. -- Mass spectrometry at the march: the place subsequent? From molecular biophysics to structural biology, views and demanding situations. -- Appendix: Physics of electrospray. summary: "Recent advances in mass spectrometry (MS) have driven the frontiers of analytical chemistry into the biophysical laboratory. accordingly, the biophysical community's recognition of MS-based equipment, used to review protein higher-order constitution and dynamics, has sped up the growth of biophysical MS." "Despite this starting to be pattern, before no unmarried textual content has provided the complete array of MS-based experimental options and methods for biophysics. Mass Spectrometry in Biophysics expertly closes this hole within the literature."."Covering the theoretical historical past and technical points of every strategy, this much-needed reference deals an unheard of evaluation of the present country of biophysical MS. Mass Spectrometry in Biophysics starts with a useful dialogue of normal biophysical options and MS-related techniques." "Fully referenced and containing a beneficial appendix at the physics of electrospray mass spectrometry, Mass Spectrometry in Biophysics additionally bargains a compelling examine the present demanding situations dealing with biomolecular MS and the aptitude functions that may most probably form its future."--BOOK JACKET
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Extra resources for Mass spectrometry in biophysics: conformation and dynamics of biomolecules
This is achieved by combining the elements of secondary structure (α-helices, β-sheets, and turns) in a unique three-dimensional arrangement, or tertiary structure. It is the tertiary structure that affords proteins their unique biological function, whether it be purely structural, the precise spatial organization of side chains to effect catalysis of a reaction, presentation of a surface or loop for signaling or inhibition, creating a cavity or groove to bind ligand, or any of the other vast range of functions that proteins can perform.
The controversy with regard to whether protein folding follows a speciﬁc pathway or whether each molecule follows a completely different trajectory to achieve its ﬁnal folded state has been elegantly resolved in the new view of protein folding (68–70). The centerpiece of this theory is the concept of a protein energy landscape in the conformational space, which is discussed in the following section. 4. 1. Protein Conformational Ensembles and Energy Landscapes: Enthalpic and Entropic Considerations Classically, a simple chemical reaction is considered to proceed along a reaction coordinate, in which chemical bonds are formed or broken in a well-deﬁned manner, with a transition state at the highest point on the energy proﬁle where bond breaking and formation are occurring, and possibly detectable metastable intermediate structures at local free energy minima.
Binding has traditionally been considered within a framework of the structure–function paradigm, a cornerstone of molecular biology for many years. It was over a hundred years ago that Fischer coined the term lock-and-key to emphasize the requirement for a stereochemical ﬁt between an enzyme and its substrate in order for binding to occur (90). The limits of this view of the binding process became obvious in the middle of the last century, when a large body of newly acquired information on enzyme kinetics appeared to be in conﬂict with the notion that “the enzyme was a rather rigid negative of the substrate and that the substrate had to ﬁt into this negative to react” (91).