9783843394031 - Understanding Tertiary Interactions In Protein Structures: Use of Computational Methods and Techniques de Bawa, Tejdeep Singh (9 resultados)

Condición: New. pp. 64.

Taschenbuch. Condición: Neu. Understanding Tertiary Interactions In Protein Structures | Use of Computational Methods and Techniques | Tejdeep Singh Bawa | Taschenbuch | 64 S. | Englisch | 2011 | LAP LAMBERT Academic Publishing | EAN 9783843394031 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.

paperback. Condición: New. NEW. SHIPS FROM MULTIPLE LOCATIONS. book.

Taschenbuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Three-dimensional structures of proteins are the support of their biological functions.Their folds are stabilized by contacts between residues.Inner protein contacts are generally described through direct atomic contacts,while contact prediction methods mainly used inter-C distances. During the process of protein folding,the amino acid residues along the polypeptide chain interact with each other in a cooperative manner to form a stable native structure.The knowledge about inter-residue interactions in protein structures is helpful to understand the mechanism of protein folding and stability.It provides valuable insights for understanding protein folding and de novo protein design.I analyzed protein contacts on a high quality non-redundant pdbs drawn from protein databank using various criteria. I have computed the average number of contacts depending on the distance threshold to define a contact.Preferential contacts between types of amino acids have been highlighted. Detailed analysis have been done concerning the proximity of contacts in the sequence,the size of the proteins and fold classes.The strongest differences have been extracted,highlighting important residues. 64 pp. Englisch.

Condición: New. Print on Demand pp. 64 2:B&W 6 x 9 in or 229 x 152 mm Perfect Bound on Creme w/Gloss Lam.

Condición: New. PRINT ON DEMAND pp. 64.

Condición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Bawa Tejdeep SinghTejdeep is currently reading for a MA degree in Biomedical Informatics at Columbia University,completed his B.Tech in Computer Science and Engineering from GGSIP University,Delhi. Tejdeep has worked as a Research As.

Taschenbuch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Three-dimensional structures of proteins are the support of their biological functions.Their folds are stabilized by contacts between residues.Inner protein contacts are generally described through direct atomic contacts,while contact prediction methods mainly used inter-C¿ distances. During the process of protein folding,the amino acid residues along the polypeptide chain interact with each other in a cooperative manner to form a stable native structure.The knowledge about inter-residue interactions in protein structures is helpful to understand the mechanism of protein folding and stability.It provides valuable insights for understanding protein folding and de novo protein design.I analyzed protein contacts on a high quality non-redundant pdbs drawn from protein databank using various criteria. I have computed the average number of contacts depending on the distance threshold to define a contact.Preferential contacts between types of amino acids have been highlighted. Detailed analysis have been done concerning the proximity of contacts in the sequence,the size of the proteins and fold classes.The strongest differences have been extracted,highlighting important residues.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 64 pp. Englisch.

Taschenbuch. Condición: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Three-dimensional structures of proteins are the support of their biological functions.Their folds are stabilized by contacts between residues.Inner protein contacts are generally described through direct atomic contacts,while contact prediction methods mainly used inter-C distances. During the process of protein folding,the amino acid residues along the polypeptide chain interact with each other in a cooperative manner to form a stable native structure.The knowledge about inter-residue interactions in protein structures is helpful to understand the mechanism of protein folding and stability.It provides valuable insights for understanding protein folding and de novo protein design.I analyzed protein contacts on a high quality non-redundant pdbs drawn from protein databank using various criteria. I have computed the average number of contacts depending on the distance threshold to define a contact.Preferential contacts between types of amino acids have been highlighted. Detailed analysis have been done concerning the proximity of contacts in the sequence,the size of the proteins and fold classes.The strongest differences have been extracted,highlighting important residues.