scholarly journals Secondary and tertiary structural differences between histone H1 molecules from calf thymus and sea-urchin (Sphaerechinus granularis) sperm

1981 ◽  
Vol 197 (3) ◽  
pp. 655-660 ◽  
Author(s):  
V Giancotti ◽  
E Russo ◽  
S Cosimi ◽  
P D Cary ◽  
C Crane-Robinson
Keyword(s):  
Structural Feature ◽  
Sea Urchin ◽  
Tertiary Structure ◽  
Histone H1 ◽  
Tryptic Digestion ◽  
Chicken Erythrocyte ◽  
Calf Thymus ◽  
Helical Content ◽  
Structural Differences ◽  
Relationship Of

Tryptic digestion of histone H1 from the sperm of the sea urchin Sphaerechinus granularis leaves a limiting peptide of approx. 80 residues that is of similar size to the limit peptide from calf thymus H1 or chicken erythrocyte H5. The S. granularis limit peptide folds to form tertiary structure similar to that of the intact parent histone H1 (shown by n.m.r. spectra), but the helical content is decreased by the digestion from 64 residues to 28. In contrast, intact calf thymus H1 and chicken erythrocyte H5 histones have only about 28 helical residues, which are preserved in their limit peptides. The extra helix in S. granularis is shown to be rapidly digested away by trypsin, and its location in histone H1 is discussed. A possible relationship of this structural feature to the length of linker DNA is proposed.

scholarly journals Preparation and characterization of histone H1 from the sperm of the sea-urchin Sphaerechinus granularis

1981 ◽  
Vol 195 (1) ◽  
pp. 171-176 ◽  
Author(s):  
V Giancotti ◽  
S Cosimi ◽  
P D Cary ◽  
C Crane-Robinson ◽  
G Geraci
Keyword(s):  
Secondary Structure ◽  
Sea Urchin ◽  
Fluorescence Spectra ◽  
Tertiary Structure ◽  
Histone H1 ◽  
Separation And Purification ◽  
Tertiary Structures ◽  
Calf Thymus ◽  
Sea Urchin Sperm

The separation and purification of histone H1 from the sperm of the sea-urchin Sphaerechinus granularis is described. Physical studies were used to compare this histone H1 molecule with H1 histones from other species. C.d. and 270 MHz n.m.r. spectroscopy indicate that, despite significant compositional differences from other sea-urchin sperm H1 histones, their secondary and tertiary structures are very similar. A large difference in helicity was, however, found between S. granularis histone H1 and calf thymus histone H1, and their n.m.r. and fluorescence spectra also differ considerably. It is concluded that secondary structure and tertiary structure have not been conserved in the evolution of the H1 histone family.

An optical rotatory dispersion study on fibrinogen and some of its derivatives

1968 ◽  
Vol 46 (6) ◽  
pp. 617-620 ◽  
Author(s):  
William D. McCubbin ◽  
Cyril M. Kay
Keyword(s):  
Tertiary Structure ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Tryptic Digestion ◽  
Optical Rotatory ◽  
Molecular Rearrangement ◽  
The Core ◽  
Helical Content ◽  
Cotton Effects ◽  
Fibrinogen Molecule

Visible and ultraviolet optical rotatory dispersion measurements were carried out on native fibrinogen and some of its derivatives. The latter include: (1) desialicized fibrinogen, (2) a large fragment of the fibrinogen molecule produced by short tryptic digestion, (3) fibrin monomer, and (4) intermediate fibrin polymers produced by the controlled thrombin proteolysis of fibrinogen. The α-helical content of native fibrinogen was deduced as 32%, and empirical calculations suggest that there is about 14% β-structure in the molecule. Sialic acid plays no significant role in the maintenance of the secondary and tertiary structure of the native molecule. No major conformational change is associated with the thrombin proteolysis of fibrinogen, although a small increase in helical content (~5%) accompanies the staggered overlap association of fibrin monomers. The "core" resulting from the controlled tryptic digestion of fibrinogen undergoes a molecular rearrangement relative to the native molecule, such that it possesses a lower α-helical content (24%) and a higher β-form value (23%). In addition, some of the additional tyrosines in the core become encompassed in regions of greater asymmetry to give rise to small aromatic Cotton effects centered around 285 mμ.

scholarly journals Precise elimination of the N-terminal domain of histone H1

1982 ◽  
Vol 203 (3) ◽  
pp. 577-582 ◽  
Author(s):  
L Böhm ◽  
P Sautière ◽  
P D Cary ◽  
C Crane-Robinson
Keyword(s):  
Tertiary Structure ◽  
Submaxillary Gland ◽  
Spectroscopic Characterization ◽  
Histone H1 ◽  
Globular Domain ◽  
Edman Degradation ◽  
Terminal Domain ◽  
C Terminus ◽  
Mouse Submaxillary Gland ◽  
Calf Thymus

The proteinase from mouse submaxillary gland was used to cleave total calf thymus histone H1 between residues 32 and 33. The C-terminal peptide, comprising residues 33 to the C-terminus, was purified and identified by amino acids analysis and Edman degradation. Spectroscopic characterization by n.m.r. for tertiary structure and by c.d. for secondary structure shows the globular domain of the parent histone H1 to be preserved intact in the peptide. It has therefore lost only the N-terminal domain and is a fragment of histone H1 comprising the globular plus C-terminal domains only. Precise elimination of only the N-terminal domain makes the fragment suitable for testing domain function in histone H1.

Intrinsic fluorescence, difference spectrophotometry and theoretical studies on tertiary structure of calf thymus histone H1

1985 ◽  
Vol 17 (2) ◽  
pp. 217-222 ◽  
Author(s):  
S.N. Khrapunov ◽  
A.F. Protas ◽  
A.V. Sivolob ◽  
A.I. Dragan ◽  
G.D. Berdyshev
Keyword(s):  
Tertiary Structure ◽  
Histone H1 ◽  
Intrinsic Fluorescence ◽  
Theoretical Studies ◽  
Calf Thymus

Torus Circumference and Thickness Parameters From a Linear DNA Size Series Suggest How Toruses Self-Assemble

1985 ◽  
Vol 43 ◽  
pp. 522-523
Author(s):  
George C. Ruben ◽  
Kenneth A. Marx
Keyword(s):  
Tertiary Structure ◽  
Dna Complexes ◽  
Tertiary Structures ◽  
Self Assembling ◽  
Double Stranded Dna ◽  
Calf Thymus ◽  
Dna Organization ◽  
Condensed Dna ◽  
Dna Size

Certain double stranded DNA bacteriophage and viruses are thought to have their DNA organized into large torus shaped structures. Morphologically, these poorly understood biological DNA tertiary structures resemble spermidine-condensed DNA complexes formed in vitro in the total absence of other macromolecules normally synthesized by the pathogens for the purpose of their own DNA packaging. Therefore, we have studied the tertiary structure of these self-assembling torus shaped spermidine- DNA complexes in a series of reports. Using freeze-etch, low Pt-C metal (10-15Å) replicas, we have visualized the microscopic DNA organization of both calf Thymus( CT) and linear 0X-174 RFII DNA toruses. In these structures DNA is circumferentially wound, continuously, around the torus into a semi-crystalline, hexagonal packed array of parallel DNA helix sections.

Mitotic arrest caused by the amino terminus of Xenopus cyclin B2

1993 ◽  
Vol 13 (3) ◽  
pp. 1480-1488
Author(s):  
H M van der Velden ◽  
M J Lohka
Keyword(s):  
Sea Urchin ◽  
Kinase Activity ◽  
Histone H1 ◽  
Amino Terminus ◽  
Protein Kinase Activity ◽  
Truncated Protein ◽  
Amino Terminal ◽  
Egg Extracts ◽  
The Stability

Progression through mitosis requires the inactivation of the protein kinase activity of the p34cdc2-cyclin complex by a mechanism involving the degradation of cyclin. We have examined the stability in Xenopus egg extracts of radiolabeled Xenopus or sea urchin B-type cyclins synthesized in reticulocyte lysates. Xenopus cyclin B2 and sea urchin cyclin B were stable in metaphase extracts from unfertilized eggs but were specifically degraded following addition of Ca2+ to the extracts. The degradation of either cyclin was inhibited by the addition of an excess of unlabeled Xenopus cyclin B2 but not by the addition of a number of control proteins. A truncated protein containing only the amino terminus of Xenopus cyclin B2, including sequences known to be essential for cyclin degradation in other species, also inhibited cyclin degradation, even though the truncated protein was stable in extracts following Ca2+ addition. The addition of the truncated protein did not stimulate histone H1 kinase activity in extracts but prevented the loss of H1 kinase activity that normally follows Ca2+ addition to metaphase extracts. When the amino-terminal fragment was added to extracts capable of several cell cycles in vitro, progression through the first mitosis was inhibited and elevated histone H1 kinase activity was maintained. These results indicate that although the amino terminus of cyclin does not contain all of the information necessary for cyclin destruction, it is capable of interacting with components of the cyclin destruction pathway and thereby preventing the degradation of full-length cyclins.

Molten globule state of human placental cystatin (HPC) at low pH conditions and the effects of trifluoroethanol (TFE) and methanol

2006 ◽  
Vol 84 (2) ◽  
pp. 126-134 ◽  
Author(s):  
Fouzia Rashid ◽  
Sandeep Sharma ◽  
M A Baig ◽  
Bilqees Bano
Keyword(s):  
Conformational Changes ◽  
Tertiary Structure ◽  
Molten Globule ◽  
Structural Features ◽  
Cd Spectroscopy ◽  
Native State ◽  
Molten Globule State ◽  
Fluorescence Measurements ◽  
Helical Content ◽  
Human Placental Cystatin

Acid-induced conformational changes were studied in human placental cystatin (HPC) in terms of circular dichroism (CD) spectroscopy, the binding of hydrophobic dye 1-anilinonapthalene-8-sulphonic acid (ANS), and intrinsic fluorescence measurements. Our results show the formation of an acid-induced molten globule state at pH 2.0, with significant secondary and tertiary interactions that resemble the native state, exposed hydrophobic regions and the effects of trifluoroethanol (TFE) and methanol in conversion of the acid-denatured state of HPC to the alcohol-induced state, which is characterized by increased helical content, disrupted tertiary structure, and the absence of hydrophobic clusters. Alcohol-induced formation of α-helical structures at pH 2.0 is evident from the increase in the ellipticity values at 222 nm, with native-like secondary structural features at 40% TFE. The increase in helical content was observed up to 80% TFE concentration. The ability of TFE (40%) to refold acid-denatured HPC to native-state conformation is also supported by intrinsic and ANS fluorescence measurements.Key words: human placental cystatin, molten globule, acid-induced state, trifluoroethanol, methanol, CD spectroscopy, ANS fluorescence, pH, protein folding.

Synthesis of Hippospongic Acid A Analogues Designed for Investigating the Structure-Activity Relationship of its Biological Activity

2000 ◽  
Vol 53 (12) ◽  
pp. 909 ◽  
Author(s):  
Yoshikazu Hiraga ◽  
Mariko Ago ◽  
Munetaka Tokumasu ◽  
Ken Kaku ◽  
Katsuo Ohkata
Keyword(s):  
Biological Activity ◽  
Carboxylic Acid ◽  
Sea Urchin ◽  
Essential Feature ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Acid Moiety ◽  
Sea Urchin Embryos ◽  
Structure Activity ◽  
Relationship Of

Analogues of hippospongic acid A, which inhibit the gastrulation of sea urchin embryos, were synthesized. From a study on structure—activity relationships, the conjugated carboxylic acid moiety was found to be an essential feature for biological activity.

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