Ok, tu mas preklad, predpokladam, ze to postnes na fore projektu, ze?
Chaperones
Chaperones are special “superior” proteins (specific for each particular protein) enabling (facilitating, stabilizing) post-translating folding of the protein into the final functional conformation. When I was questioning my biology professor if these chaperones can modify the protein against the energy gradient, into an energy disadvantageous and unstable, but functional structure (when energy stable conformation can be inactive), he said yes, that is possible.
I have some questions and I would be happy if someone could answer them:
1.Can chaperones really change the proteins into the one with energy disadvantageous structure while keeping the protein functional?
2.If yes, is Rosetta taking them into account for the simulations?
3.Is Rosetta taking into account disulphide bonding in proteins and are these bonds calculated in the computation?
Takisto myslim, ze mam aj odpoved na otazku ohladne tych krystalov:
Xtal packing je program na predpovedanie struktury proteinov. Pouziva sa na to, aby sa z krystalickych foriem predpovedali rozpustne formy. Pokial sa dobre pamatam na info z molekularky, struktura proteinu sa zistuje energetickou difrakciou krystalickeho proteinu. Ten je vo vacsine pripadov iny, ako rozpustna forma a preto Rosetta dostava odlisne vysledky - podla mna program berie do uvahy naviazane molekuly vody, ako aj interakcie s proteinmi, pripadne vnutorne vazby. Nemalo by to teda byt nic prekvapujuce. Mozno sa ale mylim, spytaj sa na fore, hadam to upresni dotycny vedec.