Latest Alpha helix Stories
The proteins actin, myosin and titin are big players in the business of muscle contraction.
Water molecules surround the genetic material DNA in a very specific way.
Researchers have developed a simple method of making short protein chains with spiral structures that can also dissolve in water, two desirable traits not often found together.
A team of scientists from The Scripps Research Institute and the University of California, San Diego (UCSD) have developed a novel technique to observe previously unknown details of how folded structures are formed from an intrinsically disordered protein.
New findings by researchers at RIKEN and the Japan Science and Technology Agency (JST) have shed light on the remarkable electrochemical response properties of an elusive class of molecular helix structures, charting a new path in the design of molecular machines and devices. (PRWeb UK) November 16, 2010 New findings by researchers at RIKEN and the Japan Science and Technology Agency (JST) have shed light on the remarkable electrochemical response properties of an elusive class of molecular...
Understanding how mixtures of proteins assemble and how to manipulate them in the laboratory has many exciting biomedical applications, such as providing scaffolds for the engineering of tissues that can replace diseased or damaged human tissues.
New York University chemists have created three-dimensional DNA structures, a breakthrough bridging the molecular world to the world where we live.
No doubt proteins are complex. Most are â€œlargeâ€ and full of interdependent branches, pockets and bends in their final folded structure.
MIT researchers who study the structure of protein-based materials with the aim of learning the key to their lightweight and robust strength have discovered that the particular arrangement of proteins that produces the sturdiest product is not the arrangement with the most built-in redundancy or the most complicated pattern.
By J, Pieter Stevens, Mark J ABSTRACT We perform atomistic simulations on a single collagen molecule to determine its intrinsic molecular strength.
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