There are ways to obtain structure of proteins from DNA, just that they're not so good if a similar structure doesn't exist in the Protein Data Bank (http://pdb.org/ already, its called homology modelling. You have the protein sequence of an unknown structure then look for similiar sequences in the 20,000 known protein structures. That's why the more structures we add to the PDB makes it easier to find structures of unknown proteins.
Sure being able to find suitable crystallization conditions for proteins is a bottleneck at the moment and this will aid in the process and add to the 20,000 plus know Protein structures, however, this is limited to certain types of proteins. A lot of really interesting proteins however are more flexible, and its this flexibility thats the key to understanding a lot of protein function. Structures derived from crystals don't give so much information about protein dynamics and molten globule like states of proteins, in fact when you crystallize proteins they tend to be locked into one conformation. Everyone in the field should keep this in mind always. A protein structure derived from a crystal structure is just a framework, its not a final representation of final function. More clues about this kind of information can be derived from NMR (Nuclear Magnetic Resonance), however the use of NMR is restricted to relatively small proteins.
This is going to help, but its not huge, the real breakthrough will come when we can model any given protein sequence on a computer and have an acurate predicated 3 diminsional structure together with it molecular motions and dynamics in real time.
Glad to see/. covering the field, its huge and its just started, we're at the begining of an exponential curve. Maybe/. should make a seperate section for this, I'd certainly be interested in contributing articles and news to such an effort.
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There are ways to obtain structure of proteins from DNA, just that they're not so good if a similar structure doesn't exist in the Protein Data Bank (http://pdb.org/ already, its called homology modelling. You have the protein sequence of an unknown structure then look for similiar sequences in the 20,000 known protein structures. That's why the more structures we add to the PDB makes it easier to find structures of unknown proteins.
Sure being able to find suitable crystallization conditions for proteins is a bottleneck at the moment and this will aid in the process and add to the 20,000 plus know Protein structures, however, this is limited to certain types of proteins. A lot of really interesting proteins however are more flexible, and its this flexibility thats the key to understanding a lot of protein function. Structures derived from crystals don't give so much information about protein dynamics and molten globule like states of proteins, in fact when you crystallize proteins they tend to be locked into one conformation. Everyone in the field should keep this in mind always. A protein structure derived from a crystal structure is just a framework, its not a final representation of final function. More clues about this kind of information can be derived from NMR (Nuclear Magnetic Resonance), however the use of NMR is restricted to relatively small proteins. This is going to help, but its not huge, the real breakthrough will come when we can model any given protein sequence on a computer and have an acurate predicated 3 diminsional structure together with it molecular motions and dynamics in real time. Glad to see /. covering the field, its huge and its just started, we're at the begining of an exponential curve. Maybe /. should make a seperate section for this, I'd certainly be interested in contributing articles and news to such an effort.