 Complementary to the field of structural genomics , protein structure prediction seeks to develop efficient ways to provide plausible models for proteins whose structures have not yet been determined experimentally . The most successful type of structure prediction , known as homology modeling , relies on the existence of a " template " structure with sequence similarity to the protein being modeled ; structural genomics ' goal is to provide sufficient representation in solved structures to model most of those that remain . Although producing accurate models remains a challenge when only distantly related template structures are available , it has been suggested that sequence alignment is the bottleneck in this process , as quite accurate models can be produced if a " perfect " sequence alignment is known . Many structure prediction methods have served to inform the emerging field of protein engineering , in which novel protein folds have already been designed . A more complex computational problem is the prediction of intermolecular interactions , such as in molecular docking and protein – protein interaction prediction . 
 Complementary to the field of structural genomics , protein structure prediction <a href='uninflect' title='1'><mark>seeks</mark></a> to develop efficient ways to provide plausible models for proteins whose structures <a href='been_done' title='2'><mark>have</mark></a> not yet been determined experimentally . The most successful type of structure prediction , known as homology modeling , <a href='uninflect' title='3'><mark>relies</mark></a> on the existence of a " template " structure with sequence similarity to the protein being modeled ; structural genomics <a href='null_genetive' title='4'><mark>'</mark></a>goal is to provide sufficient representation in solved structures to model most of those <a href='null_relcl' title='5'><mark>that</mark></a>remain . Although producing accurate models <a href='uninflect' title='6'><mark>remains</mark></a> a challenge when only distantly related template structures <a href='drop_aux' title='7'><mark>are</mark></a>available , it <a href='been_done' title='8'><mark>has</mark></a> been suggested that sequence alignment is the bottleneck in this process , as quite accurate models can be produced if a " perfect " sequence alignment is known . Many structure prediction methods <a href='been_done' title='9'><mark>have</mark></a> served to inform the emerging field of protein engineering , in which novel protein folds <a href='been_done' title='10'><mark>have</mark></a> already been designed . A more complex computational problem <a href='drop_aux' title='11'><mark>is</mark></a>the prediction of intermolecular interactions , such as in molecular docking and protein – protein interaction prediction . 
Complementary to da field of structural genomics , protein structure prediction seek to develop efficient ways to provide plausible models fa proteins whose structures done not yet been determined experimentally . The most successful type of structure prediction , known as homology modeling , rely on the existence of a " template " structure with sequence similarity to tdaprotein being modeled ; structural genomics  goal is to provide sufficient representation in solved structures to model most of those remain . Although producing accurate models remain a challenge when only distantly related template structures available , it done been suggested that sequence alignment is the bottleneck in this process , as quite accurate models can b produced if a " bumpin " sequence alignment is known . Many structure prediction methods done served to inform thdamerging field of protein engineering , in which novel protein folds done already been designed . A more complex computational problem the prediction of intermolecular interactions , such as in molecular docking and protein – protein interaction prediction .