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Evidence is accumulating that numerous membrane proteins require specific sterol structural features for function.
Additionally, biochemical and structural studies of membrane proteins require expression of large amounts of the protein in bacterial cells, and these studies are hampered by the deleterious effects of expression on cell growth.
Biophysical and structural studies of membrane proteins require milligram quantities of proteins.
Membrane proteins require a membrane-like environment to maintain their correctly folded structures and functions during and after purification.
Model simulations demonstrate that the formation and maintenance of specific organelles comprising significantly different distributions of the two membrane proteins require both a certain degree of disproportionation of the two proteins during the budding off of small unit size vesicles and a positive-cooperative kinetics of homotypic protein-protein interactions during membrane fusion.
Moreover, many membrane proteins require a lipid environment for activity.
Similar(52)
Recently, a conserved family of type I integral membrane proteins required for normal response to the Hh signal was discovered.
In a prior study employing MALDI-TOF MS to analyze human macrophages, the extraction of membrane proteins requires specific protocols and a large quantity of cells [4].
Lysosomal targeting of endocytosed membrane proteins requires specific signals, of which the best characterised is ubiquitination.
As part of the biosynthetic pathway, the production of membrane proteins requires protein folding in the endoplasmic reticulum (ER).
To yield a domain-specific polar distribution of membrane proteins in the hepatocyte plasma membrane, the distribution of newly synthesized membrane proteins requires sorting processes.
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