scholarly journals Quantitative comparison of CrkL-SH3 binding proteins from embryonic murine brain and liver: Implications for developmental signaling and the quantification of protein species variants in bottom-up proteomics

2015 ◽  
Vol 125 ◽  
pp. 104-111 ◽  
Author(s):  
Mujeeburahim Cheerathodi ◽  
James J. Vincent ◽  
Bryan A. Ballif
Keyword(s):  
Binding Proteins ◽  
Quantitative Comparison ◽  
Protein Species ◽  
Bottom Up ◽  
Developmental Signaling ◽  
Murine Brain

Calcium-binding proteins in a vorticellid contractile organelle

1975 ◽  
Vol 19 (1) ◽  
pp. 203-213
Author(s):  
W.B. Amos ◽  
L.M. Routledge ◽  
F.F. Yew
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Sodium Dodecyl ◽  
Aromatic Amino Acids ◽  
Calcium Binding Proteins ◽  
Polyacrylamide Gels ◽  
Protein Species ◽  
Low Concentrations

The proteins of the contractile spasmoneme of Zoothamnium have been examined for comparison with other motile systems. Though capable of calcium-induced contraction, glycerinated preparations of the spasmoneme contain neither actin nor tubulin at levels that can be detected in polyacrylamide gels. Sixty per cent of the protein in sodium dodecyl sulphate gels migrates in a band at a molecular weight of approximately 20,000, consisting largely of 2 similar protein species which are here given the name of spasmins. The amino acid composition of 2 spasmin fractions has been determined by a fluorimetric method. They are rich in Asx, Glx and serine, but have few aromatic amino acids and no cystine or methionine. In calcium-buffered polyacrylamide gels, it was observed that a reduction in the electrophoretic mobility of the spasmins was induced specifically by calcium (but not magnesium) at the same low concentrations as induce contraction. This indicates that the spasmins are calcium-binding proteins which may be involved directly in the calcium-induced contraction of the spasmoneme.

Novel insights into the bottom-up mass spectrometry proteomics approach for the characterization of Pt-binding proteins: The insulin-cisplatin case study

The Analyst ◽  
2010 ◽  
Vol 135 (6) ◽  
pp. 1288 ◽  
Author(s):  
Estefanía Moreno-Gordaliza ◽  
Benito Cañas ◽  
María A. Palacios ◽  
M. Milagros Gómez-Gómez
Keyword(s):  
Mass Spectrometry ◽  
Binding Proteins ◽  
Bottom Up ◽  
Proteomics Approach

scholarly journals Combined top-down and bottom-up proteomics identifies a phosphorylation site in stem-loop-binding proteins that contributes to high-affinity RNA binding

2006 ◽  
Vol 103 (9) ◽  
pp. 3094-3099 ◽  
Author(s):  
C. H. Borchers ◽  
R. Thapar ◽  
E. V. Petrotchenko ◽  
M. P. Torres ◽  
J. P. Speir ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Rna Binding ◽  
Phosphorylation Site ◽  
Top Down ◽  
Bottom Up ◽  
Stem Loop ◽  
High Affinity

Hyaluronate-Binding Proteins of Murine Brain

1990 ◽  
Vol 54 (1) ◽  
pp. 171-180 ◽  
Author(s):  
Michelle S. Marks ◽  
Gloria Chi-Rosso ◽  
Bryan P. Toole
Keyword(s):  
Binding Proteins ◽  
Murine Brain

Toward an alignment of the actin molecule within the actin filament

1983 ◽  
Vol 41 ◽  
pp. 450-451
Author(s):  
P.R. Smith ◽  
W.E. Fowler ◽  
U. Aebi
Keyword(s):  
Actin Filament ◽  
Diffraction Data ◽  
Quantitative Estimate ◽  
Molecular Model ◽  
Quantitative Comparison ◽  
Regulatory Proteins ◽  
Essential Information ◽  
X Ray ◽  
Maximum Resolution ◽  
Lack Of Information

An understanding of the specific interactions of actin with regulatory proteins has been limited by the lack of information about the structure of the actin filament. Molecular actin has been studied in actin-DNase I complexes by single crystal X-ray analysis, to a resolution of about 0.6nm, and in the electron microscope where two dimensional actin sheets have been reconstructed to a maximum resolution of 1.5nm. While these studies have shown something of the structure of individual actin molecules, essential information about the orientation of actin in the filament is still unavailable.The work of Egelman & DeRosier has, however, suggested a method which could be used to provide an initial quantitative estimate of the orientation of actin within the filament. This method involves the quantitative comparison of computed diffraction data from single actin filaments with diffraction data derived from synthetic filaments constructed using the molecular model of actin as a building block. Their preliminary work was conducted using a model consisting of two juxtaposed spheres of equal size.

The three-dimensional structure of frozen-hydrated left- and right-handed forms of bacterial flagellar filaments from an identical serotype

1986 ◽  
Vol 44 ◽  
pp. 298-299
Author(s):  
S. Trachtenberg ◽  
D. J. DeRosier
Keyword(s):  
Ionic Strength ◽  
Basal Body ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Protein Species ◽  
Liquid Environment ◽  
Bacterial Flagellum ◽  
Left And Right ◽  
Rotary Motor ◽  
Helical Parameters

The bacterial cell is propelled through the liquid environment by means of one or more rotating flagella. The bacterial flagellum is composed of a basal body (rotary motor), hook (universal coupler), and filament (propellor). The filament is a rigid helical assembly of only one protein species — flagellin. The filament can adopt different morphologies and change, reversibly, its helical parameters (pitch and hand) as a function of mechanical stress and chemical changes (pH, ionic strength) in the environment.

High resolution spot scan imaging of frozen, hydrated actin bundles with 400kV electrons

1992 ◽  
Vol 50 (1) ◽  
pp. 512-513
Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Binding Proteins ◽  
Actin Binding ◽  
Eukaryotic Cells ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Actin Bundle ◽  
Actin Bundles ◽  
3 Dimensional ◽  
Macromolecular Assembly

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.

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