Myelin exploits phase transitions to drive it's assembly
The ability to construct complex myelin sheaths around axons is one of the greatest vertebrate inventions since the hinged jaw.
The ability to construct complex myelin sheaths around axons is one of the greatest vertebrate inventions since the hinged jaw.
(Medical Xpress)—Many diseases are multifactorial and can not be understood by simple molecular associations alone. Alzheimer's disease (AD)is associated with toxic transformations in two classes of protein,amyloid beta ...
Researchers have pinpointed a catalytic trigger for the onset of Alzheimer's disease – when the fundamental structure of a protein molecule changes to cause a chain reaction that leads to the death of neurons in the brain.
May 20, 2013
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Scientists at The Scripps Research Institute (TSRI) have made a major advance in understanding how flu viruses replicate within infected cells. The researchers used cutting-edge molecular biology and electron-microscopy techniques ...
Nov 22, 2012
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Researchers have published the first highly detailed description of how neurotensin, a neuropeptide hormone which modulates nerve cell activity in the brain, interacts with its receptor. Their results suggest that neuropeptide ...
Oct 10, 2012
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Researchers funded by the National Institutes of Health have developed a new silk-based stabilizer that, in the laboratory, kept some vaccines and antibiotics stable up to temperatures of 140 degrees Fahrenheit. This provides ...
Jul 9, 2012
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Researchers at The Scripps Research Institute have uncovered the surprising details of how a powerful anti-HIV antibody grabs hold of the virus. The findings, published in Science Express on October 13, 2011, highlight a ...
Oct 13, 2011
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(Medical Xpress) -- A new study published in the Proceedings of the National Academy of Sciences shows how scientists have used a mathematical tool to possibly identify an Achilles heel in HIV which may lead to new vaccines ...
An international research team, led by Tibor Harkany and Robert Schnell at Karolinska Institutet and MedUni Vienna's Center for Brain Research, set out to find ways of influencing hormone release to reduce stress reactions ...
Apr 23, 2024
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Scientists from St Petersburg University and the University of Montpellier have developed the first software enabling the prediction of pairs of proteins in amyloid fibrils capable of co-aggregation, i.e. a process by which ...
Apr 19, 2024
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Proteins are an important class of biological macromolecules present in all biological organisms, made up of such elements as carbon, hydrogen, nitrogen, oxygen, and sulphur. All proteins are polymers of amino acids. The polymers, also known as polypeptides, consist of a sequence of 20 different L-α-amino acids, also referred to as residues. For chains under 40 residues the term peptide is frequently used instead of protein. To be able to perform their biological function, proteins fold into one, or more, specific spatial conformations, driven by a number of noncovalent interactions such as hydrogen bonding, ionic interactions, Van Der Waals forces and hydrophobic packing. In order to understand the functions of proteins at a molecular level, it is often necessary to determine the three dimensional structure of proteins. This is the topic of the scientific field of structural biology, that employs techniques such as X-ray crystallography or NMR spectroscopy, to determine the structure of proteins.
A number of residues are necessary to perform a particular biochemical function, and around 40-50 residues appears to be the lower limit for a functional domain size. Protein sizes range from this lower limit to several thousand residues in multi-functional or structural proteins. However, the current estimate for the average protein length is around 300 residues. Very large aggregates can be formed from protein subunits, for example many thousand actin molecules assemble into a microfilament.
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