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Protein-ligand interactions from molecular recognition to drug design

  • 242 Pages
  • 1.61 MB
  • 2325 Downloads
  • English

Wiley-VCH , Weinheim
Proteins., Ligands (Biochemistry), Ligand binding (Biochemistry), Ligands., Protein Binding., Drug Design., Models, Molec
Statementedited by H.-J. Böhm and G. Schneider.
SeriesMethods and principles in medicinal chemistry ;, v. 19
ContributionsBöhm, Hans-Joachim., Schneider, Gisbert, 1965-
Classifications
LC ClassificationsQP551 .P69597 2003
The Physical Object
Paginationxx, 242 p. :
ID Numbers
Open LibraryOL3705543M
ISBN 103527305211
LC Control Number2003274430
OCLC/WorldCa52317245

Hans-Joachim Bohm is the editor of Protein-Ligand Interactions: From Molecular Recognition to Drug Design, published by Wiley. Gisbert Schneider is full professor of computer-assisted drug design at ETH Zurich, Switzerland.

He studied biochemistry and computer science at the Free University of Berlin, Germany. Hans-Joachim Bohm is the editor of Protein-Ligand Interactions: From Molecular Recognition to Drug Design, published by Wiley.

Gisbert Schneider is full professor of computer-assisted drug design at ETH Zurich, Switzerland. He studied biochemistry and computer science at the Free University of Berlin, Germany.

Protein-Ligand Interactions: From Molecular Recognition to Drug Design, Volume 19 (Methods and Principles in Medicinal Chemistry): Medicine & Health Science Books 5/5(1).

Download Protein-ligand interactions from molecular recognition to drug design FB2

Protein-Ligand Interactions: From Molecular Recognition to Drug Design Hans-Joachim B?hm, Gisbert Schneider, Raimund Mannhold, Hugo Kubinyi, Gerd Folkers The lock-and-key principle formulated by Emil Fischer as early as the end of the 19th century has still not lost any of its significance for the life sciences.

This book collects computer-based methods to address drug discovery through ligand-protein recognition, via chemical space and virtual library design, docking, quantitative models, and molecular dynamics simulations, and protein structures for the identification of potential protein targets.

Protein–ligand interaction analysis is an important step of drug design and protein engineering in order to predict the binding affinity and selectivity between ligands to the target proteins. Download the eBook Protein-ligand Interactions: From Molecular Recognition to Drug Design (Methods and Principles in Medicinal Chemistry) - Hans-Joachim Bohm in PDF or EPUB format and read it directly on your mobile phone, computer or any device.

Read "Book Review: Protein–Ligand Interactions—From Molecular Recognition to Drug Design Methods. Edited by Hans‐Joachim Böhm and Gisbert Schneider, ChemBioChem" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.

Download Citation | Protein-Ligand Interactions: From Molecular Recognition to Drug Design | Introduction and ScopeAdditivity of Pairwise Interactions – The Chelate EffectGeometric Fitting: The.

Buy Protein-ligand Interactions: From Molecular Recognition to Drug Design (Methods and Principles in Medicinal Chemistry) by Hans-Joachim Böhm, Gisbert Schneider, Raimund Mannhold, Hugo Kubinyi, Gerd Folkers (ISBN: ) from Amazon's Book Store. Everyday low prices and free delivery on eligible : Hardcover.

Innovative and forward-looking, this volume focuses on recent achievements in this rapidly progressing field and looks at future potential for development. The first part provides a basic understanding of the factors governing protein-ligand interactions, followed by a comparison of key experimental methods (calorimetry, surface plasmon resonance, NMR) used in generating interaction data.

Book Title. Protein-Ligand Interactions: From Molecular Recognition to Drug Design From Molecular Recognition to Drug Design. Additional Information. How to Cite.

Höfliger, M.

Description Protein-ligand interactions from molecular recognition to drug design FB2

and Beck-Sickinger, A. () Receptor-Ligand Interaction, in Protein-Ligand Interactions: From Molecular Recognition to Drug Design (eds H.-J.

Böhm and G. Molecular Recognition of Protein−Ligand Complexes: Applications to Drug Design Synergistic Structural Information from Covalent Labeling and Hydrogen–Deuterium Exchange Mass Spectrometry for Protein–Ligand Interactions.

Analytical An Automated Strategy for Binding-Pose Selection and Docking Assessment in Structure-Based Drug by: J. Zoidakis, D. Chatziharalambous, in Reference Module in Chemistry, Molecular Sciences and Chemical Engineering, Electrospray Ionization for the Study of Noncovalent Interactions.

One of the simple methods for investigating protein–ligand interactions is to acquire the ESI mass spectrum under the solvent environment that promotes complex formation.

Care must be exercised. Title:Protein-Carbohydrate Interactions Studied by NMR: From Molecular Recognition to Drug Design VOLUME: 13 ISSUE: 8 Author(s):Maria del Carmen Fernandez-Alonso, Dolores Diaz, Manuel Alvaro Berbis, Filipa Marcelo, Javier Canada and Jesus Jimenez-Barbero Affiliation:Centro de Investigaciones Ramiro de Maeztu, 9.

A detailed understanding of the protein–ligand interactions is therefore central to understanding biology at the molecular level. Moreover, knowledge of the mechanisms responsible for the protein-ligand recognition and binding will also facilitate the discovery, design, and development of drugs.

In Protein-Ligand Interactions: Methods and Applications, leading experts with hands-on experience describe in detail a broad selection of established and emerging techniques for studying the interaction between proteins and ligands, including bulk biochemical techniques, structure analysis, spectroscopy, single-molecule studies, and.

Abstract. Computational analysis of protein–ligand interactions is of pivotal importance for drug design. Assessment of ligand binding energy allows us to have a glimpse of the potential of a small organic molecule as a ligand to the binding site of a protein target.

Protein-Ligand Interactions - ISBN: - (ebook) - von Holger Gohlke, used in generating interaction data. The second half of the book is devoted to insilico methods of modeling and predicting molecular recognition and binding, ranging from.

Protein-Ligand Interactions - I As such, a key factor in drug design is being able to anticipate the residence time that a ligand remains bound to its target. Residence time, in turn, can be directly correlated with the apparent dissociation rate of the complex.

Pos Spectroscopic Investigation Of The Molecular Recognition Mechanism. Structure-based drug design attempts to use the structure of proteins as a basis for designing new ligands by applying the principles of molecular recognition.

Selective high affinity binding to the target is generally desirable since it leads to more efficacious drugs with fewer side effects. Thus, one of the most important principles for designing or obtaining potential new ligands is to.

Flexible Protein–Ligand Docking. Flexible protein–ligand docking is a cornerstone for the discovery of new drugs. The integration of different variables allows the prediction of behavior of various chemical compounds and protein molecules and identification of drug.

A detailed understanding of the protein-ligand interactions is therefore central to understanding biology at the molecular level. Moreover, knowledge of the mechanisms responsible for the protein-ligand recognition and binding will also facilitate the discovery, design, and development of drugs.

In the present review, first, the physicochemical. Accurate modeling of protein ligand binding is an important step in structure-based drug design, is a useful starting point for finding new lead compounds or drug candidates.

The 'Lock and Key' concept of protein-ligand binding has dominated descriptions of these interactions, and has been effectively translated to computational molecular. Molecular recognition is thus a central topic in the development of active substances, since stability and specificity determine whether a substance can be used as a drug.

Nowadays, computer-aided prediction and intelligent molecular design make a large contribution to the constant search for, e.

g., improved enzyme inhibitors, and new concepts. Protein–protein interactions (PPIs) are physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific.

Böhm, H.-J. and Schneider, G. (Eds) () Protein-Ligand Interaction: From Molecular Recognition to Drug Design. Wiley-VCH, Weinheim, New York.

Details Protein-ligand interactions from molecular recognition to drug design PDF

Protein-Ligand Binding and Drug Design CMPS Crystallography and Drugs We can crystallize a protein with a potential ligand and examine the protein-ligand interactions. SAR-by-NMR Structure-Activity-Relationship or Chemical Shift Perturbation molecular modeling approaches are far from perfect,43 both the.

The molecular interactions that drive ligand-protein binding are a key to quantitatively understanding the basis of molecular recognition and to designing therapeutic interventions through rational drug design. Drug molecules usually act by binding to specific target proteins. Protein–Ligand Interactions •The extent of the drug binding into its target characterized by the binding constant •However, one should recognize that Ki is having NO units (it’s dimensionless) –if it would have a dimension, like usually mentioned (typically mol/L) the.

End-point free energy calculations using MM-GBSA and MM-PBSA provide a detailed understanding of molecular recognition in protein–ligand interactions. The binding free energy can be used to rank-order protein–ligand structures in virtual screening for compound or target identification.

Here, we carry out free energy calculations for a diverse set of 11 proteins bound to 14 small molecules.Data sets. A non-redundant set of protein-ligand complexes was extracted from the CREDO database and classified into six sets by the type of small molecule involved: approved drugs, oral drugs, synthetic small molecules (for want of a better term, see File S1), protein-protein interactions inhibitors, natural small molecules and small peptides.

These terms are used to describe the categories.Examination of Molecular Recognition in Protein-Ligand Interactions: Prospective Study and Methods Development by Yat T.

Tang Doctor of Philosophy in Computational Biology Washington University in St. Louis, Research Advisor: Professor Garland R. Marshall This dissertation is a compilation of two main projects that were investigated during.