Protein cleavage

Eiweiss-spaltung, /. cleavage of albumin protein cleavage, proteolysis, -sparmittel, n. albumin sparer protein sparer, -stoff, m. albuminous substance, protein albumen albumin, -verbindung, /. albuminous compound, protein albuminate. 

Nienhaus K, Nienhaus GU, Wiedenmann J, Nar H (2005) Structural basis for photo-induced protein cleavage and green-to-red conversion of fluorescent protein EosFP. Proc Natl Acad Sci USA 102 9156-9159... 

FRET is an extremely useful phenomenon when it comes to the analysis of molecular conformations and interactions. F or the analysis of interactions, in which two separate molecules are labeled with an appropriate pair of fluorophores, an interaction can be shown by observing FRET. Further, FRET can be used as a type of spectroscopic ruler to measure the closeness of interactions. Proteins, lipids, enzymes, DNA, and RNA can all be labeled and interactions documented. This general method can be applied not only to questions of cellular function like kinase dynamics [3] but also to disease pathways, for example, the APP-PS1 interaction that is important in Alzheimer s disease (AD) [4], Alternatively, two parts of a molecule of interest can be labeled with a donor and acceptor fluorophore. Using this technique, changes in protein conformation and differences between isoforms of proteins can be measured, as well as protein cleavage. 

Incubation of proteins in aqueous media at elevated temperatures significantly reduces the number of methylol adducts and intermolecular cross-links. Increasing pressure not only seems to accentuate this process significantly, but also appears to be accompanied by protein cleavage at aspartate residues.13... 

From a historical point of view, it is fascinating to observe how technical and theoretical development of mass spectrometry has caused the rise of proteomics. Although different ways of specific protein cleavage were well understood by the 1960s, the dramatic development of mass spectrometry at the turn of the millennium fulfilled the dream of... 

Figure 6.3 Mts-Atf-Biotin can be used to label bait proteins at available thiol groups using the MTS group, which forms a disulfide linkage after reaction. The modified protein then is allowed to interact with a protein sample and photoactivated with UV light to cause a covalent crosslink with any interacting proteins. Cleavage of the disulfide bond effectively transfers the biotin label to the unknown interacting protein.

Fig. 2. Proteolytic cleavages involved in the formation of the SFV structural proteins. Cleavages I-III take place during translation of the 26 S RNA, and cleavages IV-V during intracellular transport.

Figure 7.11 Activation of the caspase proteases during apoptosis. Caspases are implicated in both the induction and execution of the apoptotic process. Following the apoptotic stimuli, initiator caspases (caspase 8 or 9) are activated by autocatalysis. The initiator caspases then activate the effector caspases (caspase 3, 6, and 7), which are responsible for most of the protein cleavage during apoptosis.

Xu, L., and Simoni, R.D. (2003). The inhibition of degradation of 3-hydroxy-3-methyl-glutaryl coenzyme A (HMG-CoA) reductase by sterol regulatory element binding protein cleavage-activating protein requires four phenylalanine residues in span 6 of HMG-CoA reductase transmembrane domain. Arch Biochem Biophys 414 232-243. 

Fig. 8. Primary structure of retrovirus envelope proteins. Cleavage of retrovirus envelope proteins yields the two subunits SU and TM. SU is white, the fusion peptide and transmembrane segments of TM are black, and the remainder of TM is cross-hatched.

Fig. 12. Primary and tertiary structures of the Newcastle disease virus F protein. Cleavage of the precursor F protein yields the F2 (amino-terminal) and FI (carboxy-terminal) fragments. In the top schematic, F2 is white, the fusion-peptide and transmembrane segments of FI are black, and the remainder of FI is cross-hatched. In the X-ray crystallographic structure of NDV-F (Chen et at, 2001a), electron density for the fusion peptides was not visible, but the fusion peptide is at the amino terminus of FI and would therefore be expected to extend from the bottom of the...

Figure 1. Structure of the protein cleavage reagent N,N-diethylaminopropyl-bis-(3-hydroxypropyl) phosphine.

Mg-ATP can be used to disaggregate protein complexes (Otto et al., 1995 Hoyoshi et ai, 1995) so os to obtain higher amounts of protein cleavage (Pellegrini ef al., 1994). 

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