SMS 2.0: an updated database to study the structural plasticity of short peptide fragments in non-redundant proteins.

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Search and analysis of identical reverse octapeptides in unrelated proteins.

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P2860

SMS 2.0: an updated database to study the structural plasticity of short peptide fragments in non-redundant proteins.

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2012 nî lūn-bûn

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SMS 2.0: an updated database t ...... nts in non-redundant proteins.

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SMS 2.0: an updated database t ...... nts in non-redundant proteins.

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SMS 2.0: an updated database t ...... nts in non-redundant proteins.

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SMS 2.0: an updated database t ...... nts in non-redundant proteins.

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Dheeraj Ravella

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Durairaj Sherlin

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Kanagaraj Sekar

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Mani Shankar

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Marthandan Kirti Vaishnavi

http://www.w3.org/2001/XMLSchema#string

Muthukumarasamy Uthaya Kumar

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P2860

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Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels

PISCES: a protein sequence culling server

Modelling the polypeptide backbone with 'spare parts' from known protein structures.

Conserved key amino acid positions (CKAAPs) derived from the analysis of common substructures in proteins.

Persistently conserved positions in structurally similar, sequence dissimilar proteins: roles in preserving protein fold and function.

Evolution and physics in comparative protein structure modeling.

Database algorithm for generating protein backbone and side-chain co-ordinates from a C alpha trace application to model building and detection of co-ordinate errors.

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scholarly article

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10.1016/S1672-0229(11)60032-6

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2012-02-01T00:00:00Z

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221980421

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22449400

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5054494

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SMS 2.0: an updated database to study the structural plasticity of short peptide fragments in non-redundant proteins.

about

P2860

P2860

SMS 2.0: an updated database to study the structural plasticity of short peptide fragments in non-redundant proteins.

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