Structural data and biological properties of almond gum oligosaccharide: Application to beef meat preservation

A series of mini-antibodies (monovalent and bivalent Fabs) targeting the conserved internal trimeric coiled-coil of the N-heptad repeat (N-HR) of HIV-1 gp41 has been previously constructed and reported. Crystal structures of two closely related monovalent Fabs, one (Fab 8066) broadly neutralizing across a wide panel of HIV-1 subtype B and C viruses, and the other (Fab 8062) non-neutralizing, representing the extremes of this series, were previously solved as complexes with 5-Helix, a gp41 pre-hairpin intermediate mimetic. Binding of these Fabs to covalently stabilized chimeric trimers of N-peptides of HIV-1 gp41 (named (CCIZN36)3 or 3-H) has now been investigated using X-ray crystallography, cryo-electron microscopy, and a variety of biophysical methods. Crystal structures of the complexes between 3-H and Fab 8066 and Fab 8062 were determined at 2.8 and 3.0 Å resolution, respectively. Although the structures of the complexes with the neutralizing Fab 8066 and its non-neutralizing counterpart Fab 8062 were generally similar, small differences between them could be correlated with the biological properties of these antibodies. The conformations of the corresponding CDRs of each antibody in the complexes with 3-H and 5-Helix are very similar. The adaptation to a different target upon complex formation is predominantly achieved by changes in the structure of the trimer of N-HR helices, as well as by adjustment of the orientation of the Fab molecule relative to the N-HR in the complex, via rigid-body movement. The structural data presented here indicate that binding of three Fabs 8062 with high affinity requires more significant changes in the structure of the N-HR trimer compared to binding of Fab 8066. A comparative analysis of the structures of Fabs complexed to different gp41 intermediate mimetics allows further evaluation of biological relevance for generation of neutralizing antibodies, as well as provides novel structural insights into immunogen design.

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Properties of barrier shrink bags made with EVOH and polyamide for fresh beef meat preservation

Polímeros ◽

10.1590/0104-1428.04516 ◽

2018 ◽

Vol 28 (2) ◽

pp. 125-130

Author(s):

Jose Boaventura Rodrigues ◽

Kleber Brunelli ◽

Claire Isabel Grígoli de Luca Sarantopoulos ◽

Lea Mariza de Oliveira

Keyword(s):

Beef Meat ◽

Meat Preservation

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Purification, structural data and biological properties of polysaccharide fromPrunus amygdalusgum

International Journal of Food Science & Technology ◽

10.1111/ijfs.12687 ◽

2014 ◽

Vol 50 (3) ◽

pp. 578-584 ◽

Cited By ~ 36

Author(s):

Fatma Bouaziz ◽

Mohamed Koubaa ◽

Claire Boisset Helbert ◽

Fatma Kallel ◽

Dorra Driss ◽

...

Keyword(s):

Structural Data ◽

Biological Properties

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Three Dimensional structure and organization of diploid chromosomes by optical section microscopy

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100127608 ◽

1987 ◽

Vol 45 ◽

pp. 633-635

Author(s):

David A. Agard ◽

Yasushi Hiraoka ◽

John W. Sedat

Keyword(s):

Dimensional Space ◽

Three Dimensional ◽

Developmental State ◽

Mitotic Cell ◽

Biological Properties ◽

Dimensional Structure ◽

Specific Gene ◽

Three Dimensional Structure ◽

Complementary Techniques ◽

Dynamic Structures

In an effort to understand the complex relationship between structure and biological function within the nucleus, we have embarked on a program to examine the three-dimensional structure and organization of Drosophila melanogaster embryonic chromosomes. Our overall goal is to determine how DNA and proteins are organized into complex and highly dynamic structures (chromosomes) and how these chromosomes are arranged in three dimensional space within the cell nucleus. Futher, we hope to be able to correlate structual data with such fundamental biological properties as stage in the mitotic cell cycle, developmental state and transcription at specific gene loci.Towards this end, we have been developing methodologies for the three-dimensional analysis of non-crystalline biological specimens using optical and electron microscopy. We feel that the combination of these two complementary techniques allows an unprecedented look at the structural organization of cellular components ranging in size from 100A to 100 microns.

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Tubulin structure at intermediate resolution

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100140634 ◽

1995 ◽

Vol 53 ◽

pp. 852-853

Author(s):

K. H. Downing ◽

S. G. Wolf ◽

E. Nogales

Keyword(s):

High Resolution ◽

Structural Data ◽

Therapeutic Drug ◽

Zinc Ions ◽

Two Dimensional ◽

X Ray Diffraction ◽

X Ray ◽

Negative Stain ◽

Functional Mechanisms ◽

Tubulin Structure

Microtubules are involved in a host of critical cell activities, many of which involve transport of organelles through the cell. Different sets of microtubules appear to form during the cell cycle for different functions. Knowledge of the structure of tubulin will be necessary in order to understand the various functional mechanisms of microtubule assemble, disassembly, and interaction with other molecules, but tubulin has so far resisted crystallization for x-ray diffraction studies. Fortuitously, in the presence of zinc ions, tubulin also forms two-dimensional, crystalline sheets that are ideally suited for study by electron microscopy. We have refined procedures for forming the sheets and preparing them for EM, and have been able to obtain high-resolution structural data that sheds light on the formation and stabilization of microtubules, and even the interaction with a therapeutic drug.Tubulin sheets had been extensively studied in negative stain, demonstrating that the same protofilament structure was formed in the sheets and microtubules. For high resolution studies, we have found that the sheets embedded in either glucose or tannin diffract to around 3 Å.

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HRTEM study of valleriite, a hydroxide-bearing copper sulfide

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100175442 ◽

1990 ◽

Vol 48 (4) ◽

pp. 462-463

Author(s):

S. Wang ◽

P. R. Buseck

Keyword(s):

Electron Microscope ◽

High Resolution ◽

Copper Sulfide ◽

Carbonaceous Chondrite ◽

Structural Data ◽

Basic Structure ◽

Long Period ◽

Selected Area Electron Diffraction ◽

Transmission Electron ◽

Wavy Structure

Valleriite is an unusual mineral, consisting of intergrowths of sulfide layers (corresponding in structure to the mineral smythite - Fe9S11) and hydroxide layers (corresponding to brucite - Mg(OH2)). It has a composition of approximately 1.526[Mg.68Al.32(OH)2].[Fe1.07Cu.93S2] and consists of two interpenetrating lattices, each of which retains its individual structural and diffraction characteristics parallel to the layering. The valleriite structure is related to that of tochilinite, an unusual iron-rich mineral that is of considerable interest for the origin of certain carbonaceous chondrite meteorites and to those of franckeite and cylindrite, two minerals that are of interest because of their unique morphological and crystallographic properties, e.g., the distinctive curved form of cylindrite and the perfect mica-like cleavage with unusual striations and the long-period wavy structure of franckeite.Our selected-area electron diffraction (SAED) patterns and high-resolution transmission electron microscope (HRTEM) images of valleriite provide new structural data. A basic structure and a new superstructure have been observed.

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Membrane–cytoskeleton interactions in cholesterol-dependent domain formation

Essays in Biochemistry ◽

10.1042/bse0570177 ◽

2015 ◽

Vol 57 ◽

pp. 177-187 ◽

Cited By ~ 9

Author(s):

Jennifer N. Byrum ◽

William Rodgers

Keyword(s):

Biological Properties ◽

Membrane Rafts ◽

Membrane Domains ◽

Biological Functions ◽

Membrane Cytoskeleton ◽

Heterogeneous Structures ◽

Integral Role ◽

Model Cell ◽

Actomyosin Cytoskeleton ◽

Dependent Domain

Since the inception of the fluid mosaic model, cell membranes have come to be recognized as heterogeneous structures composed of discrete protein and lipid domains of various dimensions and biological functions. The structural and biological properties of membrane domains are represented by CDM (cholesterol-dependent membrane) domains, frequently referred to as membrane ‘rafts’. Biological functions attributed to CDMs include signal transduction. In T-cells, CDMs function in the regulation of the Src family kinase Lck (p56lck) by sequestering Lck from its activator CD45. Despite evidence of discrete CDM domains with specific functions, the mechanism by which they form and are maintained within a fluid and dynamic lipid bilayer is not completely understood. In the present chapter, we discuss recent advances showing that the actomyosin cytoskeleton has an integral role in the formation of CDM domains. Using Lck as a model, we also discuss recent findings regarding cytoskeleton-dependent CDM domain functions in protein regulation.

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