protein tertiary structure (33 Ergebnisse)

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Taschenbuch. Zustand: Neu. Microparticle Formation by Spray-Freeze-Drying | The Influence of Atomization Conditions on Protein Secondary and Tertiary Structure | Sebastian Vonhoff | Taschenbuch | 188 S. | Englisch | 2015 | Südwestdeutscher Verlag für Hochschulschriften | EAN 9783838117713 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.

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Taschenbuch. Zustand: Neu. The Protein Folding Problem and Tertiary Structure Prediction | Kenneth M. Jr. Merz (u. a.) | Taschenbuch | 581 S. | Englisch | 2012 | Birkhäuser | EAN 9781468468335 | Verantwortliche Person für die EU: Springer Basel AG in Springer Science + Business Media, Heidelberger Platz 3, 14197 Berlin, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu.

Zustand: New. 2012. Softcover reprint of the original 1st ed. 1994. paperback. . . . . . Books ship from the US and Ireland.

Taschenbuch. Zustand: Neu. Druck auf Anfrage Neuware - Printed after ordering - A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will make 40,000 more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional protein structures. This translation will be indispensable for the analy sis of results from the Human Genome Project, de novo protein design, and many other areas of biotechnological research. Finally, an in-depth study of the rules of protein folding should provide vital clues to the protein fold ing process. The search for these rules is therefore an important objective for theoretical molecular biology. Both experimental and theoretical ap proaches have been used in the search for a solution, with many promising results but no general solution. In recent years, there has been an exponen tial increase in the power of computers. This has triggered an incredible outburst of theoretical approaches to solving the protein folding problem ranging from molecular dynamics-based studies of proteins in solution to the actual prediction of protein structures from first principles. This volume attempts to present a concise overview of these advances. Adrian Roitberg and Ron Elber describe the locally enhanced sam pling/simulated annealing conformational search algorithm (Chapter 1), which is potentially useful for the rapid conformational search of larger molecular systems.

Taschenbuch. Zustand: Neu. Protein Tertiary Structure | Molecular Biology, Protein, Nucleic Acid Primary Structure, Amino Acid | Lambert M. Surhone (u. a.) | Taschenbuch | Englisch | 2026 | OmniScriptum | EAN 9786134668989 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.

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Taschenbuch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - High Quality Content by WIKIPEDIA articles! In biochemistry and chemistry, the tertiary structure of a protein or any other macromolecule is its three-dimensional structure, as defined by the atomic coordinates. Tertiary structure is considered to be largely determined by the protein's primary structure, or the sequence of amino acids of which it is composed. Efforts to predict tertiary structure from the primary structure are known generally as protein structure prediction. However, the environment in which a protein is synthesized and allowed to fold are significant determinants of its final shape and are usually not directly taken into account by current prediction methods. (Most such methods do rely on comparisons between the sequence to be predicted and sequences of known structure in the Protein Data Bank and thus account for environment indirectly, assuming the target and template sequences share similar cellular contexts.).

Taschenbuch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - High Quality Content by WIKIPEDIA articles! A common motif in the secondary structure of proteins, the alpha helix ( -helix) is a right- handed coiled or spiral conformation, in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier (i+4 rightarrow i hydrogen bonding). This secondary structure is also sometimes called a classic Pauling-Corey-Branson alpha helix (see below). Among types of local structure in proteins, the -helix is the most regular and the most predictable from sequence, as well as the most prevalent.

Taschenbuch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. A DNA clamp, also known as a sliding clamp, is a protein fold that serves as a processivity-promoting factor in DNA replication. As a critical component of the DNA polymerase III holoenzyme, the clamp protein binds DNA polymerase and prevents this enzyme from dissociating from the template DNA strand. The clamp-polymerase protein-protein interactions are stronger and more specific than the direct interactions between the polymerase and the template DNA strand; because the rate-limiting step in the DNA synthesis reaction is the association of the polymerase with the DNA template, the presence of the sliding clamp dramatically increases the number of nucleotides that the polymerase can add to the growing strand per association event. The presence of the DNA clamp can increase the rate of DNA synthesis up to 1,000-fold compared with a nonprocessive polymerase.

Taschenbuch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - High Quality Content by WIKIPEDIA articles! Structural biology is a branch of molecular biology, biochemistry, and biophysics concerned with the molecular structure of biological macromolecules, especially proteins and nucleic acids, how they acquire the structures they have, and how alterations in their structures affect their function. This subject is of great interest to biologists because macromolecules carry out most of the functions of cells, and because it is only by coiling into specific three-dimensional shapes that they are able to perform these functions. This architecture, the 'tertiary structure' of molecules, depends in a complicated way on the molecules' basic composition, or 'primary structures.' Structural biology is that branch of life science,which deals with the study of molecular strucuture of biological macromolecules like proteins and nucleic acids.

Taschenbuch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - High Quality Content by WIKIPEDIA articles! Structural alignment attempts to establish equivalences between two or more polymer structures based on their shape and three-dimensional conformation. This process is usually applied to protein tertiary structures but can also be used for large RNA molecules. In contrast to simple structural superposition, where at least some equivalent residues of the two structures are known, structural alignment requires no a priori knowledge of equivalent positions. Structural alignment is a valuable tool for the comparison of proteins with low sequence similarity, where evolutionary relationships between proteins cannot be easily detected by standard sequence alignment techniques.

Taschenbuch. Zustand: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will make 40,000 more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional protein structures. This translation will be indispensable for the analy sis of results from the Human Genome Project, de novo protein design, and many other areas of biotechnological research. Finally, an in-depth study of the rules of protein folding should provide vital clues to the protein fold ing process. The search for these rules is therefore an important objective for theoretical molecular biology. Both experimental and theoretical ap proaches have been used in the search for a solution, with many promising results but no general solution. In recent years, there has been an exponen tial increase in the power of computers. This has triggered an incredible outburst of theoretical approaches to solving the protein folding problem ranging from molecular dynamics-based studies of proteins in solution to the actual prediction of protein structures from first principles. This volume attempts to present a concise overview of these advances. Adrian Roitberg and Ron Elber describe the locally enhanced sam pling/simulated annealing conformational search algorithm (Chapter 1), which is potentially useful for the rapid conformational search of larger molecular systems. 596 pp. Englisch.

Zustand: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will make 40,000 more tertiary structures available for immediate study by translating the DNA sequence information in the sequence.

Taschenbuch. Zustand: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - This thesis deals with the preparation microparticles by spray-freeze-drying (SFD). As the process consists of various unit operations, the stability of labile APIs, such as proteins, can be serverly impaired. The secondary structure of a protein is known to be directly linked to its overall stability. However, quantification of protein secondary structure by FTIR spectroscopy can show poor reproducibility. Therefore, the first part of this thesis covers the development of a new FTIR method for objective and fast determination of protein secondary structure. The second part investigates the influence of atomization conditions on protein secondary and tertiary structure as well as residual enzyme activity during SFD. The process is analyzed after a) atomization b) atomization, freezing and thawing and c) the complete SFD process. A thorough comparison of the utilized ultrasound nozzles (including particle size distribution, temperatures and cavitation effects) is performed in the third part of this thesis. In the fourth and last part, different formulations containing a mixture of alpha-chymotrypsin and various excipients are evaluated for their stability.

Zustand: New. Print on Demand pp. 596.

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Taschenbuch. Zustand: Neu. This item is printed on demand - Print on Demand Titel. Neuware -A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will make 40,000 more tertiary structures available for immediate study by translating the DNA sequence information in the sequence databases into three-dimensional protein structures. This translation will be indispensable for the analy sis of results from the Human Genome Project, de novo protein design, and many other areas of biotechnological research. Finally, an in-depth study of the rules of protein folding should provide vital clues to the protein fold ing process. The search for these rules is therefore an important objective for theoretical molecular biology. Both experimental and theoretical ap proaches have been used in the search for a solution, with many promising results but no general solution. In recent years, there has been an exponen tial increase in the power of computers. This has triggered an incredible outburst of theoretical approaches to solving the protein folding problem ranging from molecular dynamics-based studies of proteins in solution to the actual prediction of protein structures from first principles. This volume attempts to present a concise overview of these advances. Adrian Roitberg and Ron Elber describe the locally enhanced sam pling/simulated annealing conformational search algorithm (Chapter 1), which is potentially useful for the rapid conformational search of larger molecular systems.Springer Nature c/o IBS, Benzstrasse 21, 48619 Heek 596 pp. Englisch.

Taschenbuch. Zustand: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware 112 pp. Englisch.

Taschenbuch. Zustand: Neu. Alpha helix | Secondary structure, Protein, Amino, Hydrogen bond, Carbonyl, Amino acid, Folding (chemistry), Beta sheet, Tertiary structure | Frederic P. Miller (u. a.) | Taschenbuch | Englisch | 2026 | OmniScriptum | EAN 9786130840105 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu Print on Demand.

Taschenbuch. Zustand: Neu. Nucleic acid design | Nucleic acid, DNA nanotechnology, DNA computing, Nucleic acid tertiary structure, Protein design, Nucleic acid secondary structure | Benoit Knútr | Taschenbuch | Englisch | 2026 | OmniScriptum | EAN 9786131692499 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu Print on Demand.

Taschenbuch. Zustand: Neu. Tertiary Structure | Biochemistry, Chemistry, Protein, Macromolecule, Primary Structure, Protein Structure Prediction, Protein Data Bank, Globular Protein, Disulfide Bond, Conformational Isomerism | Lambert M. Surhone (u. a.) | Taschenbuch | Englisch | 2026 | OmniScriptum | EAN 9786130350604 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu Print on Demand.

Taschenbuch. Zustand: Neu. DNA Clamp | Protein, Tertiary structure, Processivity, DNA replication, DNA polymerase III holoenzyme | Avery Iustinus Tim | Taschenbuch | Englisch | 2026 | OmniScriptum | EAN 9786131636684 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu Print on Demand.

Taschenbuch. Zustand: Neu. Structural Biology | Molecular Biology, Biochemistry, Biophysics, Macromolecule, Protein, Nucleic Acid, Tertiary Structure | Lambert M. Surhone (u. a.) | Taschenbuch | Englisch | 2026 | OmniScriptum | EAN 9786130352141 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu Print on Demand.

Taschenbuch. Zustand: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Please note that the content of this book primarily consists of articlesavailable from Wikipedia or other free sources online. In biochemistryand molecular biology, the tertiary structure of a protein or any othermacromolecule is its three-dimensional structure, as defined by theatomic coordinates. Tertiary structure is considered to be largelydetermined by the protein's primary structure - the sequence of aminoacids of which it is composed. Efforts to predict tertiary structurefrom the primary structure are known generally as protein structureprediction. However, the environment in which a protein is synthesizedand allowed to fold are significant determinants of its final shape andare usually not directly taken into account by current predictionmethods. Most such methods do rely on comparisons between the sequenceto be predicted and sequences of known structure in the Protein DataBank and thus account for environment indirectly, assuming the targetand template sequences share similar cellular contexts.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 112 pp. Englisch.