Update on protein structure prediction: Results of the 1995 IRBM workshop

T Hubbard; A Tramontano; G Barton; D Jones; M Sippl; A Valencia; A Lesk; J Moult; B Rost; C Sander; R Schneider; A Lahm; R Leplae; C Buta; M Eisenstein; O Fjellstrom; H Floeckner; JG Grossmann; J Hansen; MH Citterich; Flemming Steen Jørgensen; A MarchlerBauer; J Osuna; J Park; A Reinhardt; LR dePouplana; A RojoDominguez; V Saudek; J Sinclair; S Sturrock; C Venclovas; C Vinals

doi:10.1016/S1359-0278(96)00028-4

Update on protein structure prediction: Results of the 1995 IRBM workshop

T Hubbard, A Tramontano, G Barton, D Jones, M Sippl, A Valencia, A Lesk, J Moult, B Rost, C Sander, R Schneider, A Lahm, R Leplae, C Buta, M Eisenstein, O Fjellstrom, H Floeckner, JG Grossmann, J Hansen, MH CitterichFlemming Steen Jørgensen, A MarchlerBauer, J Osuna, J Park, A Reinhardt, LR dePouplana, A RojoDominguez, V Saudek, J Sinclair, S Sturrock, C Venclovas, C Vinals

16 Citationer (Scopus)

Abstract

Computational tools for protein structure prediction are of great interest to molecular, structural and theoretical biologists due to a rapidly increasing number of protein sequences with no known structure. In October 1995, a workshop was held at IRBM to predict as much as possible about a number of proteins of biological interest using ab initio pre!diction of fold recognition methods. 112 protein sequences were collected via an open invitation for target submissions. 17 were selected for prediction during the workshop and for 11 of these a prediction of some reliability could be made. We believe that this was a worthwhile experiment showing that the use of a range of independent prediction methods and thorough use of existing databases can lead to credible and useful ab initio structure predictions.

Originalsprog	Udefineret/Ukendt
Tidsskrift	Folding and Design
Vol/bind	1
Udgave nummer	3
Sider (fra-til)	R55-R63
ISSN	0969-2126
DOI	https://doi.org/10.1016/S1359-0278(96)00028-4
Status	Udgivet - 1996

Adgang til dokumentet

10.1016/S1359-0278(96)00028-4

Citationsformater

Hubbard, T., Tramontano, A., Barton, G., Jones, D., Sippl, M., Valencia, A., Lesk, A., Moult, J., Rost, B., Sander, C., Schneider, R., Lahm, A., Leplae, R., Buta, C., Eisenstein, M., Fjellstrom, O., Floeckner, H., Grossmann, JG., Hansen, J., ... Vinals, C. (1996). Update on protein structure prediction: Results of the 1995 IRBM workshop. Folding and Design, 1(3), R55-R63. https://doi.org/10.1016/S1359-0278(96)00028-4

Hubbard, T, Tramontano, A, Barton, G, Jones, D, Sippl, M, Valencia, A, Lesk, A, Moult, J, Rost, B, Sander, C, Schneider, R, Lahm, A, Leplae, R, Buta, C, Eisenstein, M, Fjellstrom, O, Floeckner, H, Grossmann, JG, Hansen, J, Citterich, MH, Jørgensen, FS, MarchlerBauer, A, Osuna, J, Park, J, Reinhardt, A, dePouplana, LR, RojoDominguez, A, Saudek, V, Sinclair, J, Sturrock, S, Venclovas, C & Vinals, C 1996, 'Update on protein structure prediction: Results of the 1995 IRBM workshop', Folding and Design, bind 1, nr. 3, s. R55-R63. https://doi.org/10.1016/S1359-0278(96)00028-4

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title = "Update on protein structure prediction: Results of the 1995 IRBM workshop",

abstract = "Computational tools for protein structure prediction are of great interest to molecular, structural and theoretical biologists due to a rapidly increasing number of protein sequences with no known structure. In October 1995, a workshop was held at IRBM to predict as much as possible about a number of proteins of biological interest using ab initio pre!diction of fold recognition methods. 112 protein sequences were collected via an open invitation for target submissions. 17 were selected for prediction during the workshop and for 11 of these a prediction of some reliability could be made. We believe that this was a worthwhile experiment showing that the use of a range of independent prediction methods and thorough use of existing databases can lead to credible and useful ab initio structure predictions.",

author = "T Hubbard and A Tramontano and G Barton and D Jones and M Sippl and A Valencia and A Lesk and J Moult and B Rost and C Sander and R Schneider and A Lahm and R Leplae and C Buta and M Eisenstein and O Fjellstrom and H Floeckner and JG Grossmann and J Hansen and MH Citterich and J{\o}rgensen, {Flemming Steen} and A MarchlerBauer and J Osuna and J Park and A Reinhardt and LR dePouplana and A RojoDominguez and V Saudek and J Sinclair and S Sturrock and C Venclovas and C Vinals",

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doi = "10.1016/S1359-0278(96)00028-4",

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TY - JOUR

T1 - Update on protein structure prediction

T2 - Results of the 1995 IRBM workshop

AU - Hubbard, T

AU - Tramontano, A

AU - Barton, G

AU - Jones, D

AU - Sippl, M

AU - Valencia, A

AU - Lesk, A

AU - Moult, J

AU - Rost, B

AU - Sander, C

AU - Schneider, R

AU - Lahm, A

AU - Leplae, R

AU - Buta, C

AU - Eisenstein, M

AU - Fjellstrom, O

AU - Floeckner, H

AU - Grossmann, JG

AU - Hansen, J

AU - Citterich, MH

AU - Jørgensen, Flemming Steen

AU - MarchlerBauer, A

AU - Osuna, J

AU - Park, J

AU - Reinhardt, A

AU - dePouplana, LR

AU - RojoDominguez, A

AU - Saudek, V

AU - Sinclair, J

AU - Sturrock, S

AU - Venclovas, C

AU - Vinals, C

PY - 1996

Y1 - 1996

N2 - Computational tools for protein structure prediction are of great interest to molecular, structural and theoretical biologists due to a rapidly increasing number of protein sequences with no known structure. In October 1995, a workshop was held at IRBM to predict as much as possible about a number of proteins of biological interest using ab initio pre!diction of fold recognition methods. 112 protein sequences were collected via an open invitation for target submissions. 17 were selected for prediction during the workshop and for 11 of these a prediction of some reliability could be made. We believe that this was a worthwhile experiment showing that the use of a range of independent prediction methods and thorough use of existing databases can lead to credible and useful ab initio structure predictions.

AB - Computational tools for protein structure prediction are of great interest to molecular, structural and theoretical biologists due to a rapidly increasing number of protein sequences with no known structure. In October 1995, a workshop was held at IRBM to predict as much as possible about a number of proteins of biological interest using ab initio pre!diction of fold recognition methods. 112 protein sequences were collected via an open invitation for target submissions. 17 were selected for prediction during the workshop and for 11 of these a prediction of some reliability could be made. We believe that this was a worthwhile experiment showing that the use of a range of independent prediction methods and thorough use of existing databases can lead to credible and useful ab initio structure predictions.

U2 - 10.1016/S1359-0278(96)00028-4

DO - 10.1016/S1359-0278(96)00028-4

M3 - Tidsskriftartikel

SN - 0969-2126

VL - 1

SP - R55-R63

JO - Structure

JF - Structure

IS - 3

ER -