Factors governing fibrillogenesis of polypeptide chains
Using lattice models we explore the factors that determine the tendencies of polypeptide chains to aggregate by exhaustively sampling the sequence and conformational space. The morphologies of the fibril-like structures and the time scales ($\tau_{fib}$) for their formation depend on a balance betwe...
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| creator | Li, Mai Suan Co, Nguyen Truong Reddy, Govardhan Hu, C-K Straub, J. E Thirumalai, D |
| description | Using lattice models we explore the factors that determine the tendencies of
polypeptide chains to aggregate by exhaustively sampling the sequence and
conformational space. The morphologies of the fibril-like structures and the
time scales ($\tau_{fib}$) for their formation depend on a balance between
hydrophobic and coulomb interactions. The extent of population of an ensemble
of \textbf{N$^*$} structures, which are fibril-prone structures in the spectrum
of conformations of an isolated protein, is the major determinant of
$\tau_{fib}$. This observation is used to determine the aggregating sequences
by exhaustively exploring the sequence space, thus providing a basis for genome
wide search of fragments that are aggregation prone. |
| doi_str_mv | 10.48550/arxiv.1011.1454 |
| format | Article |
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polypeptide chains to aggregate by exhaustively sampling the sequence and
conformational space. The morphologies of the fibril-like structures and the
time scales ($\tau_{fib}$) for their formation depend on a balance between
hydrophobic and coulomb interactions. The extent of population of an ensemble
of \textbf{N$^*$} structures, which are fibril-prone structures in the spectrum
of conformations of an isolated protein, is the major determinant of
$\tau_{fib}$. This observation is used to determine the aggregating sequences
by exhaustively exploring the sequence space, thus providing a basis for genome
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polypeptide chains to aggregate by exhaustively sampling the sequence and
conformational space. The morphologies of the fibril-like structures and the
time scales ($\tau_{fib}$) for their formation depend on a balance between
hydrophobic and coulomb interactions. The extent of population of an ensemble
of \textbf{N$^*$} structures, which are fibril-prone structures in the spectrum
of conformations of an isolated protein, is the major determinant of
$\tau_{fib}$. This observation is used to determine the aggregating sequences
by exhaustively exploring the sequence space, thus providing a basis for genome
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polypeptide chains to aggregate by exhaustively sampling the sequence and
conformational space. The morphologies of the fibril-like structures and the
time scales ($\tau_{fib}$) for their formation depend on a balance between
hydrophobic and coulomb interactions. The extent of population of an ensemble
of \textbf{N$^*$} structures, which are fibril-prone structures in the spectrum
of conformations of an isolated protein, is the major determinant of
$\tau_{fib}$. This observation is used to determine the aggregating sequences
by exhaustively exploring the sequence space, thus providing a basis for genome
wide search of fragments that are aggregation prone.</abstract><doi>10.48550/arxiv.1011.1454</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Physics - Soft Condensed Matter Quantitative Biology - Biomolecules |
| title | Factors governing fibrillogenesis of polypeptide chains |
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