Supramolecular Protein Chemistry

2020 ◽  
Keyword(s):  
Protein Chemistry

Structural and Chemical Studies of Pathological Fibers in Human Neurofibrillary Degeneration

1985 ◽  
Vol 43 ◽  
pp. 726-729
Author(s):  
K.S. Kosik ◽  
L.K. Duffy ◽  
S. Bakalis ◽  
C. Abraham ◽  
D.J. Selkoe
Keyword(s):  
Monoclonal Antibodies ◽  
Alzheimer Disease ◽  
Human Brain ◽  
Neurofibrillary Tangles ◽  
Morphological Analysis ◽  
High Specificity ◽  
Cytoskeletal Proteins ◽  
Neuritic Plaque ◽  
Protein Chemistry ◽  
Chemical Studies

The major structural lesions of the human brain during aging and in Alzheimer disease (AD) are the neurofibrillary tangles (NFT) and the senile (neuritic) plaque. Although these fibrous alterations have been recognized by light microscopists for almost a century, detailed biochemical and morphological analysis of the lesions has been undertaken only recently. Because the intraneuronal deposits in the NFT and the plaque neurites and the extraneuronal amyloid cores of the plaques have a filamentous ultrastructure, the neuronal cytoskeleton has played a prominent role in most pathogenetic hypotheses.The approach of our laboratory toward elucidating the origin of plaques and tangles in AD has been two-fold: the use of analytical protein chemistry to purify and then characterize the pathological fibers comprising the tangles and plaques, and the use of certain monoclonal antibodies to neuronal cytoskeletal proteins that, despite high specificity, cross-react with NFT and thus implicate epitopes of these proteins as constituents of the tangles.

scholarly journals Protein Chemistry and the Development of Allosterism: Jeffries Wyman

2002 ◽  
Vol 277 (46) ◽  
pp. e1-e2
Author(s):  
Robert D. Simoni ◽  
Robert L. Hill ◽  
Martha Vaughan
Keyword(s):  
Protein Chemistry

scholarly journals NeissLock provides an inducible protein anhydride for covalent targeting of endogenous proteins

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Arne H. A. Scheu ◽  
Sheryl Y. T. Lim ◽  
Felix J. Metzner ◽  
Shabaz Mohammed ◽  
Mark Howarth
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor ◽  
Binding Protein ◽  
Growth Factor Receptor ◽  
Molecular Engineering ◽  
Nucleophilic Attack ◽  
High Yield ◽  
Protein Chemistry ◽  
Transforming Growth Factor Α ◽  
Endogenous Proteins

AbstractThe Neisseria meningitidis protein FrpC contains a self-processing module (SPM) undergoing autoproteolysis via an aspartic anhydride. Herein, we establish NeissLock, using a binding protein genetically fused to SPM. Upon calcium triggering of SPM, the anhydride at the C-terminus of the binding protein allows nucleophilic attack by its target protein, ligating the complex. We establish a computational tool to search the Protein Data Bank, assessing proximity of amines to C-termini. We optimize NeissLock using the Ornithine Decarboxylase/Antizyme complex. Various sites on the target (α-amine or ε-amines) react with the anhydride, but reaction is blocked if the partner does not dock. Ligation is efficient at pH 7.0, with half-time less than 2 min. We arm Transforming Growth Factor-α with SPM, enabling specific covalent coupling to Epidermal Growth Factor Receptor at the cell-surface. NeissLock harnesses distinctive protein chemistry for high-yield covalent targeting of endogenous proteins, advancing the possibilities for molecular engineering.

Applications of gas-liquid chromatography in protein chemistry

1976 ◽  
Vol 116 (2) ◽  
pp. 305-314 ◽  
Author(s):  
Kenneth W.M. Davy ◽  
Colin J.O.R. Morris
Keyword(s):  
Liquid Chromatography ◽  
Gas Liquid Chromatography ◽  
Protein Chemistry
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