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Originally posted by bodebliss
You are not doing a myriad of things with protein folding. ...you are only testing their theories on how the proteins fold.
folding.stanford.edu...
Originally posted by bodebliss
follow the link and learn. ...They have published some papers, but as you will see while reading them , they have a narrow focus.
This doesn't change the nature of protein folding , ...The fact that protein folding can be done at all is a miracle,
Originally posted by bodebliss
The nimber 1 and 2 killers of humans do not have anything to do w/ prions.
www.kup.at...
Atherothrombosis is the underlying condition that results in events leading to myocardial infarction, ischemic stroke, and vascular death. As such, the leading cause of death of the estimated 55,694,000 people worldwide who died in 2000 was atherothrombosis, manifested as cardiovascular disease, ischemic heart disease and stroke (52% of deaths). Other main causes of death were: AIDS (5%) violent death (12%) pulmonary disease (14%) infectious diseases (19%) cancer (24%).
Originally posted by bodebliss
You don't know the people involved in the world community grid or how they will use their findings.
Originally posted by bodebliss
I remember reading on the stanford site that stanford's project is one of 2 that actually seen a protein's simulated folding. all the rest were not able to get a simulated folding of even the most simple proteins.
This whole field is baby stepping right now.
Originally posted by bodebliss
You are probably thinking of xray chromatography which is the taking of snap shots of atomic processes.
Ultrafast Spectroscopy and Dynamics of Biomolecules
www4.nationalacademies.org...
Proteins and other biomolecules are often thought of in terms of the exquisitely detailed atomic pictures revealed by x-ray crystal structures. However, x-ray crystallography only provides a representation of the average structure, or a snapshot of a single configuration. In reality, proteins are constantly fluctuating between conformers that may represent large displacements from the atomic positions shown in the crystalline form. These motions impact fundamental biochemical processes such as allostery, interactions with binding partners, susceptibilities to proteolytic cleavage, and hydrogen exchange kinetics. Therefore, a molecular-level description of biology requires an understanding of protein dynamics.
...The dynamics of biological macromolecules span an enormous range of time scales, ranging from femtoseconds (10-15 sec) to seconds. The characterization of these motions represents a formidable experimental challenge. ...We are interested in measuring the spectra of bimolecular motions, understanding the structural nature of these motions, and relating the dynamics to biological function. The laboratory employs ultrafast laser spectroscopies for measuring the femtosecond through nanosecond time scale dynamics, which underlie the slower motions. ...We will also develop a quantitative understanding of the role of femtosecond-nanosecond dynamics in the entropy changes which occur during ligand binding, folding, and other conformational transitions.
www4.nas.edu...
Unlike simple chemical reactions, protein folding is a very heterogeneous process with a large distribution of microscopic pathways connecting folded and unfolded states. Experimental determination of the distribution of these pathways requires measurements on single molecules, as ensemble measurements yield only average properties. Since it is rapidly becoming possible to fold proteins by molecular dynamics calculations, which consist of single molecule trajectories, experimental distributions are becoming essential as tests of the validity of these simulations. Up to now, single molecule folding studies have been confined almost entirely to fluorescence resonance energy transfer from intensity measurements on free diffusing molecules. The next step will be to develop methods to isolate single molecules for observation of multiple folding and unfolding events, as has already been accomplished with RNA. Expertise and advanced instrumentation exists at NIST for optical and physical studies of single molecules, such as force techniques including optical tweezers and cantilever-based molecular pullers that can be used in conjunction with optical measurements to study structural changes under an applied load. Conventional single molecule and ensemble instrumentation (for kinetic studies at nanoseconds and longer) exist at NIH, as well as expertise in theoretical and computational aspects of protein folding.
www4.nationalacademies.org...
The structure and dynamics of these proteins and polypeptides will be qualitatively assessed in microfluidic channels with spectroscopic techniques. Fluorescence resonant energy transfer (FRET) and surface enhanced Raman spectroscopy (SERS) each offer unique capabilities and insight into the difficult task of assigning protein structure. With FRET, each partner of a binding pair is labeled with a different fluorophore--one, the "donor" is bluer than the other, the "acceptor". The donor molecule is excited with a laser and begins to fluoresce; the acceptor molecule will only fluoresce if the distance between the two molecules is less than ~50 Angstroms. Therefore, it is possible to observe the tagged positions on the protein as they come in out of contact during folding or unfolding. Through the use of metallic nanoparticles fabricated in situ in the microfluidic channel, SERS provides the frequency of the vibrational bands of specific chemical groups within the protein. This inelastic photon scattering process offers a mechanism to monitor the proximity and environment of specific chemical groups, such as the carbonyl stretch, or so-called amid I band at ~1600 cm-1, which is a signature for protein conformation. Furthermore, unlike with infrared spectroscopy, it is possible to gather this vibrational data proteins in H20 media.