1^st Prague Protein's Spring

Mission

From Peptides to Proteins - evolution of structure,dynamics and interactions

1) Peptides, proteins and evolution of their structure

- prebiotic ancestors of peptides/proteins and their origin

- sequence length and composition as a determinant of the polypeptide chain structure

- local conformational preferences of amino acids in heterogeneous polypeptide chain and the consequences for protein structure

  and folding

- conformational space of small peptides, theoretical methods utilized for conformational space sampling, their accuracy and limits,

- experimental methods and peptide structures determination

2) Structural domains as the elementary units of the protein structure

- fundamental foldons - folding, stability and dynamics

- protein structure as a composition of independent domains.

- de novo design of short structural motives, polypeptides and proteins.

- Protein folding and importance of cooperativeness.

- Sequence/structure invariants of tertiary structure arrangements - hydrophobic core, sulfate bridges, salt bridges

3) Stabilizing interaction in proteins and protein complexes and their dynamics

- Sequence/structure evolution - role of particular amino acids

- Aggregation as a specific case of protein - protein interactions

- Protein - protein interaction and change of the structure and dynamics upon this event

- Correlated residue movements in proteins

- Protein folding/unfolding equilibria

- Intrinsically unstructured proteins