In summary, we developed a new method for rapid mutation scanning, s-RT-MELT that utilizes the Cel I/II (Surveyor TM ) and terminal deoxy-nucleotide transferase (TdT) enzymes to isolate and amplify mutation-containing DNA fragments without the requirement of DNA sizedependent techniques. Besides enabling highly increased throughput, multiplexed mutation screening and direct sequencing of the identified mutant DNA fragments, s-RT-MELT also retains the advantages of the Surveyor endonuclease over alternative pre-screening methods, such as reliability and identification of genetic alterations present at low (1-10%) fractions in the sample. s-RT-MELT provides a significant advancement in unknown mutation scanning in cancer research and diagnostics as well as for general medical, biological and biotechnology applications. Rapid Identification of Malaria Vaccine Candidates Based on α-Helical Coiled Coil Protein Motif To identify malaria antigens for vaccine development, we selected α-helical coiled coil domains of proteins predicted to be present in the parasite erythrocytic stage. The corresponding synthetic peptides are expected to mimic structurally “native” epitopes. Indeed the 95 chemically synthesized peptides were all specifically recognized by human immune sera, though at various prevalence. Peptide specific antibodies were obtained both by affinity-purification from malaria immune sera and by immunization of mice. These antibodies did not show significant cross reactions, i.e., they were specific for the original peptide, reacted with native parasite proteins in infected erythrocytes and several were active in inhibiting in vitro parasite growth. Circular dichroism studies indicated that the selected peptides assumed partial or high α-helical content. Thus, we demonstrate that the bioinformatics/chemical synthesis approach described here can lead to the rapid identification of molecules which target biologically active antibodies, thus identifying suitable vaccine candidates. This strategy can be, in principle, extended to vaccine discovery in a wide range of other pathogens. Human Plasmodium falciparum (Pf) infection is a dramatic public health problem. Today approximately forty percent of the world's population is at risk of malaria. Malaria causes more than 300 million acute clinical cases, and at least one million deaths annually. Ninety percent of malaria deaths occur in sub-Saharan African countries mostly among young children and pregnant women (http://rbm.who.int). Thus, there is an urgent need of a malaria vaccine. However, vaccine discovery, in general and particularly in malaria, is still a very empirical process. In fact, protective antigens do not bear any structural, physico-chemical or sequence-related characteristics that would allow their identification. For protective humoral responses, the only recognized characteristics of antigens are their antigenicity/immunogenicity and accessibility. In addition, the lack of surrogate markers of protection renders the vaccine discovery process difficult and time consuming. Hence, in spite of a constant and impressive progress in molecular biology techniques and antigen identification and expression [1, 2] , vaccine discovery is still labor-intensive, making the approach fastidious, costly and poorly adapted to highthroughput screening. Proper protein folding and solubility remain a limitation in numerous cases. Thus, overcoming the bottlenecks of manufacturing and identification of fragments/proteins, as possible targets of a protective immune response still constitute a scientific and technical challenge.