Theoretical investigations of simple model protein solutions

2000 ◽  
Author(s):  
C. Caccamo
Keyword(s):  
Simple Model ◽  
Protein Solutions ◽  
Theoretical Investigations ◽  
Model Protein

scholarly journals A topological analysis of difference topology experiments of condensin with Topoisomerases II

2019 ◽  
Author(s):  
Soojeong Kim ◽  
Isabel K. Darcy
Keyword(s):  
Simple Model ◽  
Experimental Technique ◽  
Topological Analysis ◽  
Simple Experiment ◽  
Dna Complexes ◽  
3 Dimensional ◽  
Model Protein ◽  
Summary Statement ◽  
Mu Transpososome ◽  
Dimensional Ball

ABSTRACTAn experimental technique called difference topology combined with the mathematics of tangle analysis has been used to unveil the structure of DNA bound by the Mu transpososome. However, difference topology experiments can be difficult and time-consuming. We discuss a modification that greatly simplifies this experimental technique. This simple experiment involves using a topoisomerase to trap DNA crossings bound by a protein complex and then running a gel to determine the crossing number of the knotted product(s). We develop the mathematics needed to analyze the results and apply these results to model the topology of DNA bound by 13S condensin and by the condensin MukB.SUMMARY STATEMENTTangles are used to model protein-DNA complexes: A 3-dimensional ball represents protein while strings embedded in this ball represent protein-bound DNA. We use this simple model to analyze experimental results.

scholarly journals Mechanical unfolding of a simple model protein goes beyond the reach of one-dimensional descriptions

2014 ◽  
Vol 141 (13) ◽  
pp. 135102 ◽  
Author(s):  
R. Tapia-Rojo ◽  
S. Arregui ◽  
J. J. Mazo ◽  
F. Falo
Keyword(s):  
Simple Model ◽  
One Dimensional ◽  
Model Protein

scholarly journals Expanding the Scope of Polyoxometalates as Artificial Proteases towards Hydrolysis of Insoluble Proteins

2021 ◽  
Author(s):  
Nada D. Savić ◽  
David E. Salazar Marcano ◽  
Tatjana N. Parac-Vogt
Keyword(s):  
Structural Investigation ◽  
Sodium Dodecyl ◽  
Surfactant Protein ◽  
Protein Solutions ◽  
Spectroscopic Techniques ◽  
Biological Processes ◽  
Selective Hydrolysis ◽  
Model Protein ◽  
First Time ◽  
Hydrolysis Of

Despite the enormous importance of insoluble proteins in biological processes, their structural investigation remains a challenging task. Development of artificial enzymatic catalysts would greatly facilitate elucidation of their structure as currently used enzymes in proteomics largely lose activity in the presence of surfactants, which are necessary to solubilize insoluble proteins. In this study the hydrolysis of a fully insoluble protein by a polyoxometalate complex as an artificial protease in surfactant solutions is reported for the first time. The hydrolysis of zein as a model protein was investigated in the presence of Zr(IV)-substituted Keggin-type polyoxometalate (POM), (Et2NH2)10[Zr(α-PW11O39)2], and different concentrations of the anionic surfactant sodium dodecyl sulfate (SDS). The selective hydrolysis of the protein upon incubation with the catalyst was observed, and the results indicate that hydrolytic selectivity and activity of the POM catalysts strongly depends on the concentration of surfactant. The molecular interactions between the POM catalyst and zein in the presence of SDS were explored using a combination of spectroscopic techniques which indicated competitive binding between POM and SDS towards the protein. The formation of micellar superstructures in tertiary POM/surfactant/protein solutions has been confirmed by electrical conductivity and Dynamic Light Scattering.

scholarly journals Excipient suitability for freeze-dried protein solutions

2019 ◽  
Author(s):  
Giovanna Sevilha Ferreira ◽  
Laura de Oliveira Nascimento ◽  
Danilo Costa Geraldes
Keyword(s):  
Total Protein ◽  
Visual Inspection ◽  
Protein Solutions ◽  
Total Protein Content ◽  
Protein Formulations ◽  
Freeze Dried ◽  
Collapse Temperature ◽  
Sample Characterization ◽  
Model Protein ◽  
Simplex Lattice

This work focused on pre-formulation studies for freeze-dried protein formulations, using albumin as a model protein. Two aminoacids and two sugars were selected as lyoprotectors and studied according a mixture design (simplex-lattice). Sample characterization included total protein content, collapse temperature and visual inspection. Sugar formulations collapsed, but not aminoacids, which indicate non sugar excipients as the best choice under the studied conditions.

Characterization of frozen hydrated biological specimens by low-loss EELS

1992 ◽  
Vol 50 (2) ◽  
pp. 1572-1573
Author(s):  
Songquan Sun ◽  
Richard D. Leapman
Keyword(s):  
Water Content ◽  
Direct Method ◽  
Internal Standard ◽  
Dry Weight ◽  
Dark Field ◽  
Protein Solutions ◽  
Subcellular Compartment ◽  
Differential Shrinkage ◽  
Electron Energy Loss

Analyses of ultrathin cryosections are generally performed after freeze-drying because the presence of water renders the specimens highly susceptible to radiation damage. The water content of a subcellular compartment is an important quantity that must be known, for example, to convert the dry weight concentrations of ions to the physiologically more relevant molar concentrations. Water content can be determined indirectly from dark-field mass measurements provided that there is no differential shrinkage between compartments and that there exists a suitable internal standard. The potential advantage of a more direct method for measuring water has led us to explore the use of electron energy loss spectroscopy (EELS) for characterizing biological specimens in their frozen hydrated state.We have obtained preliminary EELS measurements from pure amorphous ice and from cryosectioned frozen protein solutions. The specimens were cryotransfered into a VG-HB501 field-emission STEM equipped with a 666 Gatan parallel-detection spectrometer and analyzed at approximately −160 C.

Chaos and secular cycles in a structurally simple model society

2012 ◽  
Author(s):  
Alexander Medvinsky ◽  
Alexey Rusakov
Keyword(s):  
Simple Model

A Simple Model of Changes in Lumbar Intervertebral Angles During Sagittal Torso Flexion

2011 ◽  
Author(s):  
Riley E. Splittstoesser ◽  
Greg G. Knapik ◽  
William S. Marras
Keyword(s):  
Simple Model
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