Taiteilijaresidenssit kuvataideviennin edistäjinä : Selvitys Suomen New Yorkin kulttuuri-instituutin residenssitoiminnasta

Tämä opinnäytetyö on selvitys Suomen New Yorkin kulttuuri-instituutin taiteilijaresidenssitoiminnasta. Opinnäytetyön tavoitteena oli kehittää Suomen New Yorkin kulttuuri-instituutin taiteilijaresidenssitoimintaa. Suomen New Yorkin kulttuuri-instituutti on edistänyt suomalaisen kulttuurin tunnettavuutta Yhdysvalloissa jo yli 20 vuotta. Yksi instituutin toiminnan päälinjauksista on taiteilijaresidenssitoiminta. Instituutti kehittää jatkuvasti yhteistyöverkostojaan jotka koostuvat paikallisesta taidekentästä ja kulttuuritoimijoista. Suomen New Yorkin kulttuuri-instituutti on opinnäytetyön tilaaja. Taiteilijaresidenssitoiminnalla tarkoitetaan taiteilijan ammattimaista työskentelyä vieraassa asuin- kulttuuri- ja työympäristössä. Taiteilijaresidenssi käsitteenä on tunnettu noin sata vuotta mutta vasta viime vuosikymmeninä niistä on kasvanut merkittäviä kulttuurivaihdon keskuksia. Instituutin residenssitoiminta on yksi monista kansainvälistymisen keinoista suomalaisille kuvataiteilijoille. New Yorkin ylitsepursuava kulttuuritarjonta asettaa omat haasteensa pitkäjänteiselle suhdetoiminnalle. Kulttuurinedistämistyötä tehdään vapaan kansalaistoiminnan periaatteella, ei niinkään virallisesta kansallisesta lähtökohdasta. Tässä työssä pohditaan myös kuvataideviennin suhdetta muiden taiteenalojen vientiin ja instituutin roolia kulttuuriviennin näkökulmasta. Opinnäytetyö on kvalitatiivinen kehittämistyö jonka keskeiset tutkimusmenetelmät ovat kyselytutkimus ja teemahaastattelu. Asiantuntijahaastateltavina olivat kulttuuri-instituutin johtajaa Leena-Maija Rossi ja New Yorkissa asuva suomalainen kuvataiteilija. Kysely tehtiin instituutin taiteilijaresidensseissä vierail-leille taiteilijoille. Lähdekirjallisuutta on käytetty haastattelu– ja kyselyaineiston vertailupohjana. Opinnäytetyön lopuksi teen yhteenvedon tutkimusprosessista ja ehdotan kehittämistoimenpiteitä residenssitoiminnan kehittämiseksi. Opinnäytetyössä esitetyt kehittämistoimenpiteet ovat pohdintoja ja ehdotuksia ja varsinainen kehittämistyö jää instituutille.The purpose of this thesis was to create a development plan for the Finnish Culture Institute in New York’s artist-in-residency program. The Finnish Culture Institute in New York has contributed the awareness of Finnish culture in the United States for over 20 years. One of the main lines of the Institute's programs is the artists-in-residency program. Institute is constantly developing cooperation networks and collaboration with the local art scene and the culture field. The subscriber of the thesis is the Finnish Culture Institute in New York. The concept of Artist-in-residency program is to offer a professional working space for artist in unknown living and working environment. The residency concept is known about a hundred years, but only in recent decades it has significantly increased cultural exchange. For Finnish artists, the Institute's residency program is a way to promote an international career, or gain an international outlook on the art field. New York City's overwhelming cultural scene is a chal-lenge to create long-term cooperation and public relations. The principle is in free civil action, yet for a national basis. This study will also discuss the relationship between the exports of visual arts, the exports of other art forms, and the Institute's role in the perspective of cultural exports. In the development plan, the focus is on the visual artist's point of view. The main research methods are survey and consultant interview. The interviewed was Finnish Culture Institute in New York’s Di-rector Leena-Maija Rossi and Finnish visual artist who lives in New York. The survey was conducted in artists who have participated in Culture Institute’s artist-in-residency program. The reference litera-ture is a comparison base for interviews and survey data. At the conclusion of the study I suggest substantial development proposals and reflections on the Institute's current state and prospects for the future. Institute executes the actual development work

Expression, purification and characterization of fungal and viral recombinant proteins

This work reports the production of recombinant yeast and viral proteins in a number of diverse in vivo model systems for enzymatic and structural studies. In the first part Hsp150Δ peptide, a derivative of the yeast (Saccharomyces cerevisiae) secretory heat-shock protein Hsp150, was investigated for its ability to act as a carrier in transporting the ectodomain of rat nerve growth factor (NGFRe) out from the yeast cell. The Hsp150Δ-NGFRe fusion protein was efficiently secreted into the growth medium, where it constituted the majority of total secreted proteins. Inhibition experiments with purified Hsp150Δ-NGFRe showed that Hsp150Δ did not prevent NGFRe from folding into a ligand-binding conformation. Circular dichroism (CD) analysis revealed that the Hsp150Δ-carrier did not have any specific secondary structure, which was also suggested by NMR analysis of a synthetic polypeptide corresponding to the repetitive consensus sequence of subunit II of Hsp150. These findings suggest that Hsp150Δ can successfully act as a carrier for foreign proteins, such as NGFRe, made and secreted by S. cerevisiae. The second part of this study involved the expression and purification of an RNA animal virus, Semliki Forest virus (SFV), nonstructural proteins (Nsp1-4) using a number of in vivo protein expression systems. To ensure quantities large enough for structural and enzymatic studies of the Nsps, each of them was expressed either in bacteria (Escherichia coli) or in insect cells (Sf9). All the proteins were expressed in high quantities (10-100 mg/l), and purified by affinity and size exclusion chromatography under nondenaturing or denaturing conditions. Independent of the expression system used, all the partially purified Nsps aggregated and precipitated either upon concentration, dialysis, storing or thawing. No detergents were found that could alleviate the aggregation problem or assist in the purification process. Despite the unsuccessful purification of Nsps for structural studies, the expression and partial purification of Nsp1 and Nsp3 permitted biochemical characterization of their enzyme activities and posttranslational modifications. Point mutational analysis of the Nsp1 methyltransferase domain revealed that residue His38 was essential for the guanylyltransferase activity of Nsp1. Furthermore, residues Asp64 and Asp90 were found to be important for the methyltransferase activity of Nsp1. Phosphorylation sites in Nsp3 were determinated by point mutational analysis, electrospray ionization (ESI) and matrix assisted laser desorption ionization (MALDI) mass spectrometry (MS) as well as by phosphopeptide mapping and Edman sequencing. A phosphorylated domain (aa 320-368) was located in the C-terminal, non-conserved region of Nsp3, where 12 serines and 4 threonines could be modified by phosphates. The phosphorylation of Nsp3 seemed not to affect the membrane association or the localization of Nsp3 in either transfected or infected cells. Furthermore, Nsp3 phosphorylation deficient mutant viruses were capable of replication in infected mammalian cells a similar manner to the wild type SFV, but their neuropathogenicity in adult mice was greatly reduced.reviewe

Variation ontology: annotator guide.

Systematic representation of information related to genetic and non-genetic variations is required to allow large scale studies, data mining and data integration, and to make it possible to reveal novel relationships between genotype and phenotype. Although lots of variation data is available it is often difficult to use due to lack of systematics

Solubility of proteins

Solubility is a fundamental protein property that has important connotations for therapeutics and use in diagnosis. Solubility of many proteins is low and affect heterologous overexpression of proteins, formulation of products and their stability. Two processes are related to soluble and solid phase relations. Solubility refers to the process where proteins have correctly folded structure, whereas aggregation is related to the formation of fibrils, oligomers or amorphous particles. Both processes are related to some diseases. Amyloid fibril formation is one of the characteristic features in several neurodegenerative diseases, but it is related to many other diseases, including cancers. Severe complex V deficiency and cataract are examples of diseases due to reduced protein solubility. Methods and approaches are described for prediction of protein solubility and aggregation, as well as predictions of consequences of amino acid substitutions. Finally, protein engineering solutions are discussed. Protein solubility can be increased, although such alterations are relatively rare and can lead to trade-off with some other properties. The aggregation prediction methods mainly aim to detect aggregation-prone sequence patches and then making them more soluble. The solubility predictors utilize a wide spectrum of features.</p

Types and effects of protein variations.

Variations in proteins have very large number of diverse effects affecting sequence, structure, stability, interactions, activity, abundance and other properties. Although protein-coding exons cover just over 1 % of the human genome they harbor an disproportionately large portion of disease-causing variants. Variation ontology (VariO) has been developed for annotation and description of variation effects, mechanisms and consequences. A holistic view for variations in proteins is made available along with examples of real cases. Protein variants can be of genetic origin or emerge at protein level. Systematic names are provided for all variation types, a more detailed description can be made by explaining changes to protein function, structure and properties. Examples are provided for the effects and mechanisms, usually in relation to human diseases. In addition, the examples are selected so that protein 3D structural changes, when relevant, are included and visualized. Here, systematics is described for protein variants based on VariO. It will benefit the unequivocal description of variations and their effects and further reuse and integration of data from different sources

Phylogeny of Tec Family Kinases: Identification of a Pre-Metazoan Origin of Btk, Bmx, Itk, Tec, Txk and the Btk Regulator SH3BP5

It is generally considered mammals and birds have five Tec family kinases (TFKs): Btk, Bmx (also known as Etk), Itk, Tec, and Txk (also known as Rlk). Here, we discuss the domains and their functions and regulation in TFKs. Over the last few years, a large number of genomes from various phyla have been sequenced making it possible to study evolutionary relationships at the molecular and sequence level. Using bioinformatics tools, we for the first time demonstrate that a TFK ancestor exists in the unicellular choanoflagellate Monosiga brevicollis, which is the closest known relative to metazoans with a sequenced genome. The analysis of the genomes for sponges, insects, hagfish, and frogs suggests that these species encode a single TFK. The insect form has a divergent and unique N-terminal region. Duplications generating the five members took place prior to the emergence of vertebrates. Fishes have two or three forms and the platypus, Ornithorhynchus anatinus, has four (lacks Txk). Thus, not all mammals have all five TFKs. The single identified TFK in frogs is an ortholog of Tec. Bmx seems to be unique to mammals and birds. SH3BP5 is a negative regulator of Btk. It is conserved in choanoflagellates and interestingly exists also in nematodes, which do not express TFKs, suggesting a broader function in addition to Btk regulation. The related SH3BP5-like protein is not found in Nematodes

Spectrum of disease-causing mutations in protein secondary structures

<p>Abstract</p> <p>Background</p> <p>Most genetic disorders are linked to missense mutations as even minor changes in the size or properties of an amino acid can alter or prevent the function of the protein. Further, the effect of a mutation is also dependent on the sequence and structure context of the alteration.</p> <p>Results</p> <p>We investigated the spectrum of disease-causing missense mutations in secondary structure elements in proteins with numerous known mutations and for which an experimentally defined three-dimensional structure is available. We obtained a comprehensive map of the differences in mutation frequencies, location and contact energies, and the changes in residue volume and charge – both in the mutated (original) amino acids and in the mutant amino acids in the different secondary structure types. We collected information for 44 different proteins involved in a large number of diseases. The studied proteins contained a total of 2413 mutations of which 1935 (80%) appeared in secondary structures. Differences in mutation patterns between secondary structures and whole proteins were generally not statistically significant whereas within the secondary structural elements numerous highly significant features were observed.</p> <p>Conclusion</p> <p>Numerous trends in mutated and mutant amino acids are apparent. Among the original residues, arginine clearly has the highest relative mutability. The overall relative mutability among mutant residues is highest for cysteine and tryptophan. The mutability values are higher for mutated residues than for mutant residues. Arginine and glycine are among the most mutated residues in all secondary structures whereas the other amino acids have large variations in mutability between structure types. Statistical analysis was used to reveal trends in different secondary structural elements, residue types as well as for the charge and volume changes.</p

Prediction of disease-related mutations affecting protein localization

<p>Abstract</p> <p>Background</p> <p>Eukaryotic cells contain numerous compartments, which have different protein constituents. Proteins are typically directed to compartments by short peptide sequences that act as targeting signals. Translocation to the proper compartment allows a protein to form the necessary interactions with its partners and take part in biological networks such as signalling and metabolic pathways. If a protein is not transported to the correct intracellular compartment either the reaction performed or information carried by the protein does not reach the proper site, causing either inactivation of central reactions or misregulation of signalling cascades, or the mislocalized active protein has harmful effects by acting in the wrong place.</p> <p>Results</p> <p>Numerous methods have been developed to predict protein subcellular localization with quite high accuracy. We applied bioinformatics methods to investigate the effects of known disease-related mutations on protein targeting and localization by analyzing over 22,000 missense mutations in more than 1,500 proteins with two complementary prediction approaches. Several hundred putative localization affecting mutations were identified and investigated statistically.</p> <p>Conclusion</p> <p>Although alterations to localization signals are rare, these effects should be taken into account when analyzing the consequences of disease-related mutations.</p