Protein Structure and Functions - W 1400-216BKWN-W
Ribosome and mechanism of translation. Mechanisms of fidelity maintenance during protein synthesis. Protein folding. Levinthal paradox. Folding pathways. Folding of multidomain proteins. Posttranslational and cotranslational folding. Chaperones: cooperation and selectivity. Small (holding) chaperones and chaperonins. Misfolding and aggregation. Amyloid fibrils. Cross-beta structure. Aggregating sequences. Amyloid diseases. Prion disorders. Functional amyloids. Neutralization of misfolded proteins. Intrinsically disordered (unstructured) proteins. Proteins of thermophiles. Protein transport. Signal sequences. Gated transport (import through nuclear pores). Transmembrane transport. Vesicular transport. Posttranslational and cotranslational transport. Cell-penetrating peptides. Protein domains as compact, spatially distinct units; as regions with assigned functions; as significantly sequence-similar homologs. Symmetry as the rule for proteins. Homo- and heterooligomers. Advantages of symmetrical over asymmetrical proteins. Membrane proteins. Structural motifs of membrane proteins. Insertion of proteins into membranes. Translocons. Folding of membrane proteins. Topology of membrane proteins. Multi-spanning proteins. Domain movement in proteins. Allostery. Phosphorylation-dependent conformational transitions. Molecular machines. ATP synthase. ATPase motors. The light-driven proton pump (bacteriorhodopsin). Protein-nucleic acid interactions. Examples of DNA- and RNA-binding domains. DNA topology. Supercoils, catenanes, knots. Linking number, writhing number and twisting number. Type I and type II topoisomerases. Distribution of DNA topology in bacterial cells and DNA gyrase. Hyperthermophilic organisms and reverse gyrase. Eukaryotic topoisomerases. Topoisomerases as targets for antibiotics and anticancer drugs. Protein-protein interactions and protein complexes. Regulation of protein-protein interactions. Platform proteins. Protein networks. Moonlighting proteins: examples, switch between functions, contribution to human diseases. The minimum set of proteins necessary to sustain a functioning cell. Protein degradation. Proteases, peptidases, proteinases. Serine, cysteine, aspartate proteinases; metallo proteinases. Intramembrane-cleaving proteases. Lysosomes. Degradation rates of proteins. Proteasomes. Ubiquitination of proteins. Apoptotic degradation of proteins.
Type of course
elective monographs
Mode
Prerequisites (description)
Course coordinators
Learning outcomes
Having completed the course the student of Biotechnology (molecular biotechnology):
- Has broad knowledge in the fields of the structure, folding, functioning and degradation of proteins (S2_W01).
- Has up-to-date knowledge in the fields of the structure, folding, functioning and degradation of proteins (S2_W01).
- Is familiar with the rules of research planning, techniques and metodology used in the fields of the structure, folding, functioning and degradation of proteins (S2_W04).
-Has knowledge sufficient for using electronic resources and scientific literature devoted to the structure, folding, functioning and degradation of proteins, both in Polish and in English (S2_U01).
- Is able to draw proper conclusions and interpret research results found in these resources and scientific literature (S2_U01).
- Is able to study on his/her own and focus on the study area (S2_U04).
- Is careful and critical when acquiring and interpreting knowledge in the field of the structure, folding, functioning and degradation of proteins (S2_K01).
- Understand the need for informing the public about the latest achievements concerning the structure, folding, functioning and degradation of proteins, and is able to pass this knowledge in an intelligible way (S2_K02).
Having completed the course the student of Biology (general microbiology):
- Has broad knowledge in the fields of the structure, folding, functioning and degradation of proteins (S1_W01).
- Has up-to-date knowledge in the fields of the structure, folding, functioning and degradation of proteins (S1_W01).
- Is familiar with the rules of research planning, techniques and metodology used in the fields of the structure, folding, functioning and degradation of proteins (S1_W03).
-Has knowledge sufficient for using electronic resources and scientific literature devoted to the structure, folding, functioning and degradation of proteins, both in Polish and in English (S1_U01).
- Is able to draw proper conclusions and interpret research results found in these resources and scientific literature (S1_U01).
- Is able to study on his/her own and focus on the study area (S1_U04).
- Is careful and critical when acquiring and interpreting knowledge in the field of the structure, folding, functioning and degradation of proteins (S1_K01).
- Understand the need for informing the public about the latest achievements concerning the structure, folding, functioning and degradation of proteins, and is able to pass this knowledge in an intelligible way (S1_K02).
Assessment criteria
Exam is in a written form.
Practical placement
No.
Bibliography
C. Branden, J. Tooze "Introduction to protein structure" Garland Publishing.
A.M. Lesk "Introduction to protein science. Architecture, function, genomics" Oxford University Press.
A.D. Bates, A. Maxwell "DNA topology" Oxford University Press.
Additional information
Additional information (registration calendar, class conductors, localization and schedules of classes), might be available in the USOSweb system: