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Hydrophobic-hydrophilic forces and their effects on protein structural similarity

Monash University
Abdul Sattar (Aggregated by) Bela Stantic (Aggregated by) Tamjidul Hoque (Aggregated by) Trent Higgs (Aggregated by)
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=info:doi10.4225/03/5a13709f243b5&rft.title=Hydrophobic-hydrophilic forces and their effects on protein structural similarity&rft.identifier=https://doi.org/10.4225/03/5a13709f243b5&rft.publisher=Monash University&rft.description=Hydrophobic-hydrophilic interactions have a strong impact on the three-dimensional structure a protein will adopt. Because structure, not amino acid sequence order, carry out certain functions it is important to understand how these forces affect the protein folding process. In recent years, a lot of focus has been dedicated towards ab initio protein folding prediction, which tries to predict a proteins native conformation from its sequence alone. To aid this type of prediction sub-conformations from already known proteins are used to limit the free energy conformational search space. In this paper we looked into the sub-conformations’ hydrophobic-hydrophilic nature by incorporating a HP approach and proposed a way of evaluating how these type of forces affect the protein folding process. By doing this, we can gain insight into how hydrophobic-hydrophilic interactions affect protein structural similarity, and thus aid us in picking more suitable sub-conformations based off their HP shape for use in protein structure prediction. PRIB 2008 proceedings found at: http://dx.doi.org/10.1007/978-3-540-88436-1 Contributors: Monash University. Faculty of Information Technology. Gippsland School of Information Technology ; Chetty, Madhu ; Ahmad, Shandar ; Ngom, Alioune ; Teng, Shyh Wei ; Third IAPR International Conference on Pattern Recognition in Bioinformatics (PRIB) (3rd : 2008 : Melbourne, Australia) ; Coverage: Rights: Copyright by Third IAPR International Conference on Pattern Recognition in Bioinformatics. All rights reserved.&rft.creator=Abdul Sattar&rft.creator=Bela Stantic&rft.creator=Tamjidul Hoque&rft.creator=Trent Higgs&rft.date=2017&rft_rights=In Copyright&rft_subject=Bioinformatics -- Congresses&rft_subject=Computational biology -- Congresses&rft_subject=Computer vision in medicine -- Congresses&rft_subject=Computational biology -- Methods -- Congresses&rft_subject=Pattern recognition, automated -- Methods -- Congresses&rft_subject=2008&rft_subject=conference paper&rft_subject=1959.1/63678&rft_subject=monash:7847&rft_subject=Bioinformatics&rft_subject=Pattern Recognition and Data Mining&rft_subject=Bioinformatics Software&rft.type=dataset&rft.language=English Access the data
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Hydrophobic-hydrophilic interactions have a strong impact on the three-dimensional structure a protein will adopt. Because structure, not amino acid sequence order, carry out certain functions it is important to understand how these forces affect the protein folding process. In recent years, a lot of focus has been dedicated towards ab initio protein folding prediction, which tries to predict a proteins native conformation from its sequence alone. To aid this type of prediction sub-conformations from already known proteins are used to limit the free energy conformational search space. In this paper we looked into the sub-conformations’ hydrophobic-hydrophilic nature by incorporating a HP approach and proposed a way of evaluating how these type of forces affect the protein folding process. By doing this, we can gain insight into how hydrophobic-hydrophilic interactions affect protein structural similarity, and thus aid us in picking more suitable sub-conformations based off their HP shape for use in protein structure prediction. PRIB 2008 proceedings found at: http://dx.doi.org/10.1007/978-3-540-88436-1 Contributors: Monash University. Faculty of Information Technology. Gippsland School of Information Technology ; Chetty, Madhu ; Ahmad, Shandar ; Ngom, Alioune ; Teng, Shyh Wei ; Third IAPR International Conference on Pattern Recognition in Bioinformatics (PRIB) (3rd : 2008 : Melbourne, Australia) ; Coverage: Rights: Copyright by Third IAPR International Conference on Pattern Recognition in Bioinformatics. All rights reserved.

Issued: 2017-11-21

Created: 2017-11-21

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1959.1/63678 | 2008 | Bioinformatics | Bioinformatics -- Congresses | Bioinformatics Software | Computational biology -- Congresses | Computational biology -- Methods -- Congresses | Computer vision in medicine -- Congresses | Pattern Recognition and Data Mining | Pattern recognition, automated -- Methods -- Congresses | conference paper | monash:7847 |

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ACN 633 798 857