Synopsis
Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. A common motif in the secondary structure of proteins, the alpha helix (α-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 α-helix is the most regular and the most predictable from sequence, as well as the most prevalent.
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Alpha helix
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Taschenbuch. Etat : Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -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. 96 pp. Englisch. N° de réf. du vendeur 9786130840105
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Alpha helix : Secondary structure, Protein, Amino, Hydrogen bond, Carbonyl, Amino acid, Folding (chemistry), Beta sheet, Tertiary structure
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Taschenbuch. Etat : 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. N° de réf. du vendeur 9786130840105
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Alpha helix | Secondary structure, Protein, Amino, Hydrogen bond, Carbonyl, Amino acid, Folding (chemistry), Beta sheet, Tertiary structure
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Taschenbuch. Etat : 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. N° de réf. du vendeur 113250531
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Alpha helix
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Taschenbuch. Etat : 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. A common motif inthe secondary structure of proteins, the alpha helix (¿-helix) is aright- handed coiled or spiral conformation, in which every backbone N-Hgroup donates a hydrogen bond to the backbone C=O group of the aminoacid four residues earlier (i+4 rightarrow i hydrogen bonding). Thissecondary structure is also sometimes called a classicPauling-Corey-Branson alpha helix (see below). Among types of localstructure in proteins, the ¿-helix is the most regular and the mostpredictable from sequence, as well as the most prevalent.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 96 pp. Englisch. N° de réf. du vendeur 9786130840105
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