Quaternary Structure Analysis of a Hemoglobin Core in Hemoglobin–Albumin Cluster

2018 ◽  
Vol 122 (50) ◽  
pp. 12031-12039 ◽  
Author(s):  
Yoshitsugu Morita ◽  
Taiga Yamada ◽  
Moeka Kureishi ◽  
Kiyohito Kihira ◽  
Teruyuki Komatsu
Keyword(s):  
Structure Analysis ◽  
Quaternary Structure

scholarly journals Beyond BLASTing: Tertiary and Quaternary Structure Analysis Helps Identify Major Vault Proteins

2012 ◽  
Vol 5 (1) ◽  
pp. 217-232 ◽  
Author(s):  
Toni K. Daly ◽  
Andrew J. Sutherland-Smith ◽  
David Penny
Keyword(s):  
Structure Analysis ◽  
Quaternary Structure

Purification, crystallization and quaternary structure analysis of a glycerol dehydrogenase S305C mutant fromBacillus stearothermophilus

2001 ◽  
Vol 57 (1) ◽  
pp. 165-167 ◽  
Author(s):  
Jacky Burke ◽  
Sergey N. Ruzheinikov ◽  
Sveta Sedelnikova ◽  
Patrick J. Baker ◽  
David Holmes ◽  
...  
Keyword(s):  
Structure Analysis ◽  
Quaternary Structure ◽  
Glycerol Dehydrogenase

Crystallization and quaternary structure analysis of an Lrp-like regulatory protein from the hyperthermophilePyrococcus furiosus

2001 ◽  
Vol 57 (6) ◽  
pp. 886-888 ◽  
Author(s):  
Svetlana E. Sedelnikova ◽  
Sander H. J. Smits ◽  
Philip M. Leonard ◽  
Arie B. Brinkman ◽  
John van der Oost ◽  
...  
Keyword(s):  
Structure Analysis ◽  
Quaternary Structure ◽  
Regulatory Protein

Crystallization and Quaternary Structure Analysis of the NAD+-dependent Leucine Dehydrogenase from Bacillus sphaericus

1994 ◽  
Vol 236 (2) ◽  
pp. 663-665 ◽  
Author(s):  
Andrew P. Turnbull ◽  
Stephen R. Ashford ◽  
Patrick J. Baker ◽  
David W. Rice ◽  
Fiona H. Rodgers ◽  
...  
Keyword(s):  
Structure Analysis ◽  
Quaternary Structure ◽  
Bacillus Sphaericus ◽  
Leucine Dehydrogenase

A comparison of X-ray small-angle scattering results to crystal structure analysis and other physical techniques in the field of biological macromolecules

1978 ◽  
Vol 11 (1) ◽  
pp. 39-70 ◽  
Author(s):  
O. Kratky ◽  
I. Pilz
Keyword(s):  
Crystal Structure ◽  
Structure Analysis ◽  
Small Angle ◽  
Quaternary Structure ◽  
Heavy Atom ◽  
Crystal Structure Analysis ◽  
Small Angle Scattering ◽  
Biological Macromolecules ◽  
X Ray ◽  
Angle Scattering

In principle, there exist two ways to contribute to structure determination of macromolecules by X-ray diffraction: (a) by analysing diffraction data obtained from the crystalline state, and (b) by interpretation of X-ray small-angle scattering from particles in solution.The brilliant achievements of X-ray crystal-structure analysis of macromolecules, initiated by the works of Perutz on heamoglobin and Kendrew on myoglobin, are well known and it is evident that its detailed elution of secondary, tertiary and quaternary structure cannot be matched by any other means. However, a number of necessary prerequisites for a successful application, as, for example, the availability of well-defined crystals and heavy atom labelled derivatives thereof to surmount the problem of phase determination are not always given.

scholarly journals Algebraic Bayesian Network Secondary Structure Cycles Elimination Based on its Quaternary Structure Analysis

2014 ◽  
Vol 2 (21) ◽  
pp. 143 ◽  
Author(s):  
Andrey Alexandrovich Filchenkov ◽  
Konstantin Vladislavovich Frolenkov ◽  
Alexander Lvovich Tulupyev
Keyword(s):  
Secondary Structure ◽  
Bayesian Network ◽  
Structure Analysis ◽  
Quaternary Structure

Quaternary structure of Limulus polyphemus hemocyanin

1978 ◽  
Vol 36 (2) ◽  
pp. 176-177
Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen
Keyword(s):  
Electron Microscopy ◽  
Functional Properties ◽  
Horseshoe Crab ◽  
Temperature Jump ◽  
Quaternary Structure ◽  
Crystallographic Analysis ◽  
Limulus Polyphemus ◽  
Oxygen Binding ◽  
X Ray ◽  
Intact Molecule

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.

Characterization of Tamm-Horsfall Urinary Glycoprotein

1973 ◽  
Vol 31 ◽  
pp. 420-421
Author(s):  
John P. Robinson ◽  
J. David Puett
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Normal Adult ◽  
Morphological Properties ◽  
Adult Males ◽  
Circular Dichroïsm ◽  
Urinary Glycoprotein

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.

200kv superconducting cryo electron microscope

1987 ◽  
Vol 45 ◽  
pp. 642-643
Author(s):  
M. Iwatsuki ◽  
Y. Kokubo ◽  
Y. Harada ◽  
J. Lehman
Keyword(s):  
Electron Microscope ◽  
Structure Analysis ◽  
Organic Materials ◽  
Strong Interactions ◽  
Specimen Preparation ◽  
Great Effort ◽  
Electron Microscopic ◽  
Crystal Fields ◽  
Special Skill ◽  
Long Time

In recent years, the electron microscope has been significantly improved in resolution and we can obtain routinely atomic-level high resolution images without any special skill. With this improvement, the structure analysis of organic materials has become one of the interesting targets in the biological and polymer crystal fields.Up to now, X-ray structure analysis has been mainly used for such materials. With this method, however, great effort and a long time are required for specimen preparation because of the need for larger crystals. This method can analyze average crystal structure but is insufficient for interpreting it on the atomic or molecular level. The electron microscopic method for organic materials has not only the advantage of specimen preparation but also the capability of providing various information from extremely small specimen regions, using strong interactions between electrons and the substance. On the other hand, however, this strong interaction has a big disadvantage in high radiation damage.

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