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Advanced Spectroscopic Methods to Study Biomolecular Structure and
Dynamics presents the latest emerging technologies in spectroscopy
and advances in established spectroscopic methods. The book
presents a guide to research methods in biomolecular spectroscopy,
providing comprehensive coverage of developments in the
spectroscopic techniques used to study protein structure and
dynamics. Seventeen chapters from leading researchers cover key
aspects of spectroscopic methods, with each chapter covering
structure, folding, and dynamics. This title will help researchers
keep up-to-date on the latest novel methods and advances in
established methods.
Advances in Protein Molecular and Structural Biology Methods offers
a complete overview of the latest tools and methods applicable to
the study of proteins at the molecular and structural level. The
book begins with sections exploring tools to optimize recombinant
protein expression and biophysical techniques such as fluorescence
spectroscopy, NMR, mass spectrometry, cryo-electron microscopy, and
X-ray crystallography. It then moves towards computational
approaches, considering structural bioinformatics, molecular
dynamics simulations, and deep machine learning technologies. The
book also covers methods applied to intrinsically disordered
proteins (IDPs)followed by chapters on protein interaction
networks, protein function, and protein design and engineering. It
provides researchers with an extensive toolkit of methods and
techniques to draw from when conducting their own experimental
work, taking them from foundational concepts to practical
application.
This book discusses a broad range of basic and advanced topics in
the field of protein structure, function, folding, flexibility, and
dynamics. Starting with a basic introduction to protein
purification, estimation, storage, and its effect on the protein
structure, function, and dynamics, it also discusses various
experimental and computational structure determination approaches;
the importance of molecular interactions and water in protein
stability, folding and dynamics; kinetic and thermodynamic
parameters associated with protein-ligand binding; single molecule
techniques and their applications in studying protein folding and
aggregation; protein quality control; the role of amino acid
sequence in protein aggregation; muscarinic acetylcholine
receptors, antimuscarinic drugs, and their clinical significances.
Further, the book explains the current understanding on the
therapeutic importance of the enzyme dopamine beta hydroxylase;
structural dynamics and motions in molecular motors; role of
cathepsins in controlling degradation of extracellular matrix
during disease states; and the important structure-function
relationship of iron-binding proteins, ferritins. Overall, the book
is an important guide and a comprehensive resource for
understanding protein structure, function, dynamics, and
interaction.
This book discusses a broad range of basic and advanced topics in
the field of protein structure, function, folding, flexibility, and
dynamics. Starting with a basic introduction to protein
purification, estimation, storage, and its effect on the protein
structure, function, and dynamics, it also discusses various
experimental and computational structure determination approaches;
the importance of molecular interactions and water in protein
stability, folding and dynamics; kinetic and thermodynamic
parameters associated with protein-ligand binding; single molecule
techniques and their applications in studying protein folding and
aggregation; protein quality control; the role of amino acid
sequence in protein aggregation; muscarinic acetylcholine
receptors, antimuscarinic drugs, and their clinical significances.
Further, the book explains the current understanding on the
therapeutic importance of the enzyme dopamine beta hydroxylase;
structural dynamics and motions in molecular motors; role of
cathepsins in controlling degradation of extracellular matrix
during disease states; and the important structure-function
relationship of iron-binding proteins, ferritins. Overall, the book
is an important guide and a comprehensive resource for
understanding protein structure, function, dynamics, and
interaction.
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