4 edition of The Protein folding problem and tertiary structure prediction found in the catalog.
The Protein folding problem and tertiary structure prediction
Includes bibliographical references and index.
|Statement||Kenneth M. Merz, Jr., Scott M. Le Grand, editors.|
|Contributions||Merz, Kenneth M. 1959-, Le Grand, Scott M.|
|LC Classifications||QP551 .P6958216 1994|
|The Physical Object|
|Pagination||x, 581 p. :|
|Number of Pages||581|
|LC Control Number||93041522|
The Protein Folding Problem and Tertiary Structure Prediction pp | Cite as Computational Complexity, Protein Structure Prediction, and the Levinthal Paradox AuthorsCited by: This book covers elements of both the data-driven comparative modeling approach to structure prediction and also recent attempts to simulate folding using explicit or simplified models. Despite the unsolved mystery of how a protein folds, advances are being made in predicting the interactions of proteins with other : Hardcover.
A solution to the protein folding problem will m more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional protein by: 7. Protein structure prediction: | | ||| | Constituent amino-acids can be analyzed to predict sec World Heritage Encyclopedia, the aggregation of the largest online encyclopedias available, and the most definitive collection ever assembled.
Secondary structure prediction has been around for almost a quarter of a century. The early methods suffered from a lack of data. Predictions were performed on single sequences rather than families of homologous sequences, and there were relatively few known 3D structures from which to derive parameters. Many structure prediction methods have served to inform the emerging field of protein engineering, in which novel protein folds have already been designed. A more complex computational problem is the prediction of intermolecular interactions, such as in molecular docking and protein–protein interaction prediction.
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A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will m more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional proteinBrand: Birkhäuser Basel.
A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will m more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional protein by: A solution to the protein folding problem has eluded researchers for more than 30 years.
The stakes are high. Such a solution will m more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional protein structures.
editors define 'the protein folding problem' in terms of "tertiary structure prediction". As a consequence, the topics treated, e.g. in the AAAS Selected Symposium 89 (edited by D.B. Wetlaufer) are ignored. The same holds for the 'kinetics' and 'pathways' of folding; proteinAuthor: Rainer Jaenicke.
(PS)2: protein structure prediction server predicts the three-dimensional structures of protein complexes based on comparative modeling; furthermore, this server examines the coupling between subunits of the predicted complex by combining structural and evolutionary considerations.
The predicted complex structure could be indicated and. Since then, the protein folding problem has come to be regarded as three different problems: (a) the folding code: the thermodynamic question of what balance of interatomic forces dictates the structure of the protein, for a given amino acid sequence; (b) protein structure prediction: the computational problem of how to predict a protein’s Cited by: The "dead-end elimination" theorem: a new approach to the side-chain packing problem / Johan Desmet, Marc De Maeyer, and Ignace Lasters --Short structural motifs: definition, identification, and applications / Ron Unger --In search of protein folds / Manfred J.
Sippl, Sabine Weitckus, and Hannes Flöckner --An adaptive branch-and-bound. Get this from a library. The Protein folding problem and tertiary structure prediction.
[Kenneth M Merz; Scott M Le Grand;] -- A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will m more tertiary structures available for immediate study.
Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner. It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from a random coil.
Each protein exists as an unfolded. The Genetic Algorithm and Protein Tertiary Structure Prediction / Scott M. Le Grand and Kenneth M. Merz, Jr. -- 5. Conformational Search and Protein Folding / Robert E.
Bruccoleri -- 6. Building Protein Folds Using Distance Geometry: Towards a General Modeling and Prediction Method / William R. Taylor and Andras Aszodi -- 7. The prediction of protein secondary structures is an intermediate goal for determining its tertiary structure.
The analysis on the performance of several secondary structure prediction methods in Author: Michael Gromiha. Restraint free ab initio protein folding. The most general approach attempts to predict protein tertiary structure from sequence without any recourse to known protein structures or evolutionary information.
This is the traditional approach to the solution of the protein folding problem. We term this approach restraint free ab initio protein. Protein tertiary structure prediction is a research field which aims to create models and software tools able to predict the three-dimensional shape of protein molecules by describing the spatial disposition of each of its atoms starting from the sequence of its amino acids.
There exist exact methods to resolve the molecular structure with high. Tertiary structure is when the alpha-helix and beta-sheet fold onto globular structures.
Quaternary structure is when 2 or more peptide chains that have already been folded combine with each other. Prediction. The prediction of protein folds usually involves determining the tertiary (most common form) structure from its primary form.
The protein structure prediction is of three categories: homology modeling, fold recognition and ab initio modeling, and this division into categories depends on whether similar protein structures.
This paper discusses the mathematical formulation of and solution attempts for the so-called protein folding problem. The static aspect is concerned with how to predict the folded (native, tertiary) structure of a protein given its sequence of amino by: The holy grail in protein folding research has always been to predict the tertiary structure of a protein given its primary sequence.
A similar but conceptually easier problem is to design a protein which will fold to a given structure with predicted secondary structure. The Protein Folding Problem and Tertiary Structure Prediction by Jr.
Kenneth M. Merz,available at Book Depository with free delivery worldwide. The PSIPRED Protein Structure Prediction Server aggregates several of our structure prediction methods into one location.
Users can submit a protein sequence, perform the prediction of their choice and receive the results of the prediction via e-mail.
keywords: protein structure prediction, tertiary structure, tertiary structure prediction. SAM. Abstract. The polypeptide chain of globular protein is linear, but the three-dimensional of tertiary structure is quite contorted.
This was apparent from the first crystallographic determination of the structure of a protein by Kendrew et al. The contortion arises because of the need to satisfy a multitude of conflicting interactions: the hydrogen-bonding requirements of buried Cited by:. Protein structure prediction is the prediction of the three-dimensional structure of a protein from its amino acid sequence — that is, the prediction of its folding and its secondary, tertiary, and quaternary structure from its primary structure.
Structure prediction is fundamentally different from the inverse problem of protein design.The prediction of the tertiary three-dimensional structure of a protein from the primary sequence of amino acids in a protein.
This unsolved problem derived its complexity from the large number of possible configurations each bond angle can have. Abstract. RNA 3D structure prediction is analogous to the protein folding problem, particularly the astronomical size of the conformational search space and the challenge of appropriately scoring native versus decoy by: