Download e-book for iPad: Fortschritte der Chemie Organischer Naturstoffe / Progress by R. B. Corey, R. E. Marsh (auth.), L. Zechmeister (eds.)

By R. B. Corey, R. E. Marsh (auth.), L. Zechmeister (eds.)

ISBN-10: 3709171342

ISBN-13: 9783709171349

ISBN-10: 3709171350

ISBN-13: 9783709171356

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Extra resources for Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products

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4. 5. 6. 7. 8. COREY, R. : X-Ray Diffraction Studies of Crystalline Amino Acids and Peptides. Fortschr. Chern. organ. Naturstoffe 8, 310 (1951). COREY, R. B. and L. PAULING: Fundamental Dimensions of Polypeptide Chains. Proc. Roy. Soc. (London) B 141, 10 (1953). EDSALL, J. , P. J. FLORY, J. C. KENDREW, A. M. LIQUORI, G. NEMETHY, G. N. RAMACHANDRAN and H. A. SCHERAGA: A Proposal of Standard Conventions and Nomenclature for the Description of Polypeptide Conformations. J. Mol. BioI. 15, 399 (1966); J.

A more detailed description of the ribonuclease molecule is in preparation. The structure of ribonuclease-S has recently been determined by WYCKOFF, RICHARDS and their collaborators at Yale University. This enzyme is formed by the hydrolysis of the peptide bond between residues 20 and 21 or 21 and 22 of bovine pancreatic ribonuclease-A. 5 A is described in a series of three articles. The first article (I37) describes the design of a diffractometer and flow cell system which was used for the collection of the X-ray intensity data and discusses some of its applications to the crystal chemistry of ribonuclease-So The cell consists of a small polyethylene tube held in a brass yoke which is firmly attached to a standard goniometer head.

0 A found in horse oxyhemoglobin. The dimensions of the hole surrounding the two-fold axis at the center of the molecule were also in agreement with the former and different from the latter structure. These results suggest strongly that the reduced forms of horse and human hemoglobin have very similar structures, which differ from the oxyhemoglobins in the arrangement of the ,B-chains. Hemoglobin H is one of the abnormal human hemoglobins. Its molecule consists of four ,B-chains and its heme groups react with oxygen independently of each other.

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Fortschritte der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products by R. B. Corey, R. E. Marsh (auth.), L. Zechmeister (eds.)


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