DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. DIP original experiment: DIP-250132X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. DIP original experiment: DIP-250134X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. DIP original experiment: DIP-250130X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. DIP original experiment: DIP-250135X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. DIP original experiment: DIP-250133X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. DIP original experiment: DIP-250136X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Khan MQ., Sweeting B., Mulligan VK., Arslan PE., Cashman NR., Pai EF., Chakrabartty A. DIP original experiment: DIP-250131X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. prio_mesau Major prion protein PrP27-30 PrP33-35C PRNP PRP protein protein mesau Mesocricetus auratus (Golden hamster) Golden hamster MANLSYWLLALFVAMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRSSAVLFSSPPVILLISFLIFLMVG DIP protein P04273 original sequence version: 95 DIP protein P04273 original sequence version: 100 DIP protein P04273-1 original sequence version: 104 442C0E3ED4D20672 prio_mouse Major prion protein PrP27-30 PrP33-35C Prnp Prn-p Prp protein protein mouse Mus musculus Mouse MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG DIP protein P04925 original sequence version: 157 DIP protein P04925 original sequence version: 140 DIP protein P04925 original sequence version: 122 DIP protein P04925 original sequence version: 117 DIP protein P04925 original sequence version: 132 DIP protein P04925 original sequence version: 128 D5331E6321826CC0 prio_rabit Major prion protein PRNP PRP PrP27-30 PrP33-35C protein protein rabit Oryctolagus cuniculus (Rabbit) Rabbit MAHLGYWMLLLFVATWSDVGLCKKRPKPGGGWNTGGSRYPGQSSPGGNRYPPQGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGTHNQWGKPSKPKTSMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVDQYSNQNSFVHDCVNITVKQHTVTTTTKGENFTETDIKIMERVVEQMCITQYQQESQAAYQRAAGVLLFSSPPVILLISFLIFLIVG DIP protein Q95211 original sequence version: 83 prio_canlf Major prion protein PRNP PRP protein protein canlf Canis familiaris (dog) Canis lupus familiaris Dog Canis familiaris MVKSHIGSWILVLFVAMWSDVGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHSQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYLLGSAMSRPLIHFGNDCEDRYYRENMYRYPNQVYYRSVDQYNNQSTFVHDCVNITVKQHTVTTTKGENFTETDIKMMERVVEQMCITQYQRESEAYYQRGASVILFSSPPVILLVSFLIFLIVG DIP protein O46501 original sequence version: 75 b5b2h1_horse Major prion protein protein protein horse Equus caballus (Horse) Horse MVKSHVGGWILVLFVATWSDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGSHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGNDYEDRYYRENMYRYPNQVYYRPVSEYSNQNNFVHDCVNITVKQHTVTTTTKGENFTETDVKIMERVVEQMCITQYQKEYEAFQQRGASVVLFSSPPVVLLIFFLIFLIVG 78D1CB804A9B344A hoprp-1 5 12 unspecified role unspecified role unspecified role unspecified role Region 90-231 Region 90-231 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction prnp-23 3 8 unspecified role unspecified role unspecified role unspecified role Region 90-231 Region 90-231 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction prnp-24 2 11 unspecified role unspecified role unspecified role unspecified role Region 90-231 Region 90-231 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction prnp-25 7 9 unspecified role unspecified role unspecified role unspecified role Region 90-231 Region 90-231 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction prnp-26 4 8 unspecified role unspecified role unspecified role unspecified role Region 90-231 Region 90-231 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction prnp-27 1 10 unspecified role unspecified role unspecified role unspecified role Region 90-231 Region 90-231 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction prnp-28 6 10 unspecified role unspecified role unspecified role unspecified role Region 121-231 Region 121-231 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction