Many Copies (many + copy)

Distribution by Scientific Domains


Selected Abstracts


Calculating credibility: print culture, trust and economic figures in early eighteenth-century England1

ECONOMIC HISTORY REVIEW, Issue 4 2007
NATASHA GLAISYER
Credit in early modern England has been studied by both social historians of the market and historians of the book. The intersection of these literatures is explored by asking the question: how did producers of books about interest (which was closely connected to credit) convince readers that their books could be trusted? One particular book is considered: a palm-sized book of interest calculations by John Castaing. Most importantly, and unusually, many copies of this book contain his signature, which, it is argued, must be interpreted in the context of the particular role that signatures played in guaranteeing financial transactions. [source]


Crossing numbers of sequences of graphs II: Planar tiles

JOURNAL OF GRAPH THEORY, Issue 4 2003
Benny Pinontoan
Abstract We describe a method of creating an infinite family of crossing-critical graphs from a single small planar map, the tile, by gluing together many copies of the tile together in a circular fashion. This method yields all known infinite families of k -crossing-critical graphs. Furthermore, the method yields new infinite families, which extend from (4,6) to (3.5,6) the interval of rationals r for which there is, for some k, an infinite sequence of k -crossing-critical graphs all having average degree r. © 2003 Wiley Periodicals, Inc. J Graph Theory 42: 332,341, 2003 [source]


Theoretical aspects of virus capsid assembly

JOURNAL OF MOLECULAR RECOGNITION, Issue 6 2005
Adam Zlotnick
Abstract A virus capsid is constructed from many copies of the same protein(s). Molecular recognition is central to capsid assembly. The capsid protein must polymerize in order to create a three-dimensional protein polymer. More than structure is required to understand this self-assembly reaction: one must understand how the pieces come together in solution. Copyright © 2005 John Wiley & Sons, Ltd. [source]


Type II dehydroquinase: molecular replacement with many copies

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 1 2008
Kirsty Anne Stewart
Type II dehydroquinase is a small (150-amino-acid) protein which in solution packs together to form a dodecamer with 23 cubic symmetry. In crystals of this protein the symmetry of the biological unit can be coincident with the crystallographic symmetry, giving rise to cubic crystal forms with a single monomer in the asymmetric unit. In crystals where this is not the case, multiple copies of the monomer are present, giving rise to significant and often confusing noncrystallographic symmetry in low-symmetry crystal systems. These different crystal forms pose a variety of challenges for solution by molecular replacement. Three examples of structure solutions, including a highly unusual triclinic crystal form with 16 dodecamers (192 monomers) in the unit cell, are described. Four commonly used molecular-replacement packages are assessed against two of these examples, one of high symmetry and the other of low symmetry; this study highlights how program performance can vary significantly depending on the given problem. In addition, the final refined structure of the 16-dodecamer triclinic crystal form is analysed and shown not to be a superlattice structure, but rather an F -centred cubic crystal with frustrated crystallographic symmetry. [source]