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Zeitschriftentitel: | ACM SIGEVOlution |
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In: | ACM SIGEVOlution, 4, 2010, 3, S. 20-21 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Association for Computing Machinery (ACM)
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Schlagwörter: |
author_facet |
Goldstein, Moshe Goldstein, Moshe |
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author |
Goldstein, Moshe |
spellingShingle |
Goldstein, Moshe ACM SIGEVOlution Dissertation corner Electrical and Electronic Engineering Building and Construction |
author_sort |
goldstein, moshe |
spelling |
Goldstein, Moshe 1931-8499 Association for Computing Machinery (ACM) Electrical and Electronic Engineering Building and Construction http://dx.doi.org/10.1145/1731888.1731891 <jats:p> A key factor in the properties of biological molecules is their structure. This research has focused on the problem of <jats:italic>protein structure prediction</jats:italic> due to the critical role of peptides and proteins in the normal biological functionality of cells and organisms. At sufficiently low temperatures, though not always, the structure of the minimal free energy corresponds to the global minimum of its force field (FF) -- its Potential Energy Surface (PES), which is a function expressing the potential energy interactions inside the molecule. The problem of predicting the <jats:italic>native</jats:italic> (or <jats:italic>folded</jats:italic> ) structure of a polypeptide given its sequence or some unfolded structure <jats:italic>is</jats:italic> the problem of finding that global minimum. This problem is computationally hard because we know that a polypeptide's PES has an estimated number of minima, exponential on its sequence length. </jats:p> Dissertation corner ACM SIGEVOlution |
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Association for Computing Machinery (ACM) |
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ACM SIGEVOlution |
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title |
Dissertation corner |
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Dissertation corner |
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Dissertation corner |
title_fullStr |
Dissertation corner |
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Dissertation corner |
title_short |
Dissertation corner |
title_sort |
dissertation corner |
topic |
Electrical and Electronic Engineering Building and Construction |
url |
http://dx.doi.org/10.1145/1731888.1731891 |
publishDate |
2010 |
physical |
20-21 |
description |
<jats:p>
A key factor in the properties of biological molecules is their structure. This research has focused on the problem of
<jats:italic>protein structure prediction</jats:italic>
due to the critical role of peptides and proteins in the normal biological functionality of cells and organisms. At sufficiently low temperatures, though not always, the structure of the minimal free energy corresponds to the global minimum of its force field (FF) -- its Potential Energy Surface (PES), which is a function expressing the potential energy interactions inside the molecule. The problem of predicting the
<jats:italic>native</jats:italic>
(or
<jats:italic>folded</jats:italic>
) structure of a polypeptide given its sequence or some unfolded structure
<jats:italic>is</jats:italic>
the problem of finding that global minimum. This problem is computationally hard because we know that a polypeptide's PES has an estimated number of minima, exponential on its sequence length.
</jats:p> |
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author | Goldstein, Moshe |
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description | <jats:p> A key factor in the properties of biological molecules is their structure. This research has focused on the problem of <jats:italic>protein structure prediction</jats:italic> due to the critical role of peptides and proteins in the normal biological functionality of cells and organisms. At sufficiently low temperatures, though not always, the structure of the minimal free energy corresponds to the global minimum of its force field (FF) -- its Potential Energy Surface (PES), which is a function expressing the potential energy interactions inside the molecule. The problem of predicting the <jats:italic>native</jats:italic> (or <jats:italic>folded</jats:italic> ) structure of a polypeptide given its sequence or some unfolded structure <jats:italic>is</jats:italic> the problem of finding that global minimum. This problem is computationally hard because we know that a polypeptide's PES has an estimated number of minima, exponential on its sequence length. </jats:p> |
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spelling | Goldstein, Moshe 1931-8499 Association for Computing Machinery (ACM) Electrical and Electronic Engineering Building and Construction http://dx.doi.org/10.1145/1731888.1731891 <jats:p> A key factor in the properties of biological molecules is their structure. This research has focused on the problem of <jats:italic>protein structure prediction</jats:italic> due to the critical role of peptides and proteins in the normal biological functionality of cells and organisms. At sufficiently low temperatures, though not always, the structure of the minimal free energy corresponds to the global minimum of its force field (FF) -- its Potential Energy Surface (PES), which is a function expressing the potential energy interactions inside the molecule. The problem of predicting the <jats:italic>native</jats:italic> (or <jats:italic>folded</jats:italic> ) structure of a polypeptide given its sequence or some unfolded structure <jats:italic>is</jats:italic> the problem of finding that global minimum. This problem is computationally hard because we know that a polypeptide's PES has an estimated number of minima, exponential on its sequence length. </jats:p> Dissertation corner ACM SIGEVOlution |
spellingShingle | Goldstein, Moshe, ACM SIGEVOlution, Dissertation corner, Electrical and Electronic Engineering, Building and Construction |
title | Dissertation corner |
title_full | Dissertation corner |
title_fullStr | Dissertation corner |
title_full_unstemmed | Dissertation corner |
title_short | Dissertation corner |
title_sort | dissertation corner |
title_unstemmed | Dissertation corner |
topic | Electrical and Electronic Engineering, Building and Construction |
url | http://dx.doi.org/10.1145/1731888.1731891 |