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Direct prediction of profiles of sequences compatible with a protein structure by neural networks with fragment-based local and energy-based nonlocal profiles
Direct prediction of profiles of sequences compatible with a protein structure by neural networks with fragment-based local and energy-based nonlocal profiles
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Direct prediction of profiles of sequences compatible with a protein structure by neural networks with fragment-based local and energy-based nonlocal profiles

Proteins, structure, function, and bioinformatics, 2014-10, Vol.82 (10), p.2565-2573 [Peer Reviewed Journal]

2014 Wiley Periodicals, Inc. ;ISSN: 0887-3585 ;EISSN: 1097-0134 ;DOI: 10.1002/prot.24620 ;PMID: 24898915

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2
Comparing three stochastic search algorithms for computational protein design: Monte Carlo, replica exchange Monte Carlo, and a multistart, steepest-descent heuristic
Comparing three stochastic search algorithms for computational protein design: Monte Carlo, replica exchange Monte Carlo, and a multistart, steepest-descent heuristic
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Comparing three stochastic search algorithms for computational protein design: Monte Carlo, replica exchange Monte Carlo, and a multistart, steepest-descent heuristic

Journal of computational chemistry, 2016-07, Vol.37 (19), p.1781-1793 [Peer Reviewed Journal]

2016 Wiley Periodicals, Inc. ;Copyright Wiley Subscription Services, Inc. Jul 15, 2016 ;Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0192-8651 ;EISSN: 1096-987X ;DOI: 10.1002/jcc.24393 ;PMID: 27197555 ;CODEN: JCCHDD

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3
Using knowledge of protein structural constraints to predict the evolution of HIV-1
Using knowledge of protein structural constraints to predict the evolution of HIV-1
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Using knowledge of protein structural constraints to predict the evolution of HIV-1

ISSN: 0022-2836 ;EISSN: 1089-8638 ;DOI: 10.1016/j.jmb.2011.04.037

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4
Computational protein design: Software implementation, parameter optimization, and performance of a simple model
Computational protein design: Software implementation, parameter optimization, and performance of a simple model
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Computational protein design: Software implementation, parameter optimization, and performance of a simple model

Journal of computational chemistry, 2008-05, Vol.29 (7), p.1092-1102 [Peer Reviewed Journal]

Copyright © 2007 Wiley Periodicals, Inc. ;Copyright 2007 Wiley Periodicals, Inc. ;Copyright John Wiley and Sons, Limited May 2008 ;Distributed under a Creative Commons Attribution 4.0 International License ;ISSN: 0192-8651 ;EISSN: 1096-987X ;DOI: 10.1002/jcc.20870 ;PMID: 18069664 ;CODEN: JCCHDD

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5
The protein threading problem with sequence amino acid interaction preferences is NP-complete
The protein threading problem with sequence amino acid interaction preferences is NP-complete
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The protein threading problem with sequence amino acid interaction preferences is NP-complete

Protein engineering, 1994-09, Vol.7 (9), p.1059-1068 [Peer Reviewed Journal]

1994 INIST-CNRS ;ISSN: 1741-0126 ;ISSN: 0269-2139 ;EISSN: 1741-0134 ;EISSN: 1460-213X ;DOI: 10.1093/protein/7.9.1059 ;PMID: 7831276 ;CODEN: PRENE9

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6
Long- and short-range interactions in native protein structures are consistent/minimally frustrated in sequence space
Long- and short-range interactions in native protein structures are consistent/minimally frustrated in sequence space
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Long- and short-range interactions in native protein structures are consistent/minimally frustrated in sequence space

Proteins, structure, function, and bioinformatics, 2003-01, Vol.50 (1), p.35-43 [Peer Reviewed Journal]

Copyright © 2002 Wiley‐Liss, Inc. ;Copyright 2002 Wiley-Liss, Inc. ;ISSN: 0887-3585 ;EISSN: 1097-0134 ;DOI: 10.1002/prot.10242 ;PMID: 12471597

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7
Identifying sequence–structure pairs undetected by sequence alignments
Identifying sequence–structure pairs undetected by sequence alignments
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Identifying sequence–structure pairs undetected by sequence alignments

Protein engineering, 2000-07, Vol.13 (7), p.459-475 [Peer Reviewed Journal]

Oxford University Press 2000 ;Copyright Oxford University Press(England) Jul 2000 ;ISSN: 0269-2139 ;ISSN: 1741-0126 ;EISSN: 1460-213X ;EISSN: 1741-0134 ;DOI: 10.1093/protein/13.7.459 ;PMID: 10906342

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8
Robustness and efficiency in inverse protein folding
Robustness and efficiency in inverse protein folding
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Robustness and efficiency in inverse protein folding

Physica. D, 1997-09, Vol.107 (2), p.199-203 [Peer Reviewed Journal]

1997 ;ISSN: 0167-2789 ;EISSN: 1872-8022 ;DOI: 10.1016/S0167-2789(97)00087-0

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9
Inverse protein folding by the residue pair preference profile method: estimating the correctness of alignments of structurally compatible sequences
Inverse protein folding by the residue pair preference profile method: estimating the correctness of alignments of structurally compatible sequences
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Inverse protein folding by the residue pair preference profile method: estimating the correctness of alignments of structurally compatible sequences

Protein engineering, 1995-07, Vol.8 (7), p.627-639 [Peer Reviewed Journal]

ISSN: 1741-0126 ;ISSN: 0269-2139 ;EISSN: 1741-0134 ;EISSN: 1460-213X ;DOI: 10.1093/protein/8.7.627 ;PMID: 8577692

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10
Protein sequence-structure compatibility criteria in terms of statistical hypothesis testing
Protein sequence-structure compatibility criteria in terms of statistical hypothesis testing
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Protein sequence-structure compatibility criteria in terms of statistical hypothesis testing

Protein engineering, 1997-06, Vol.10 (6), p.635-646 [Peer Reviewed Journal]

ISSN: 0269-2139 ;ISSN: 1741-0126 ;EISSN: 1460-213X ;EISSN: 1741-0134 ;DOI: 10.1093/protein/10.6.635 ;PMID: 9278276

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11
Xylanase homology modeling using the inverse protein folding approach
Xylanase homology modeling using the inverse protein folding approach
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Xylanase homology modeling using the inverse protein folding approach

Protein science, 1996-04, Vol.5 (4), p.705-708 [Peer Reviewed Journal]

Copyright © 1996 The Protein Society ;ISSN: 0961-8368 ;EISSN: 1469-896X ;DOI: 10.1002/pro.5560050415 ;PMID: 8845760

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12
A study of combined structure/sequence profiles
A study of combined structure/sequence profiles
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A study of combined structure/sequence profiles

Folding & design, 1996-01, Vol.1 (6), p.451-461 [Peer Reviewed Journal]

1996 Elsevier Ltd ;ISSN: 1359-0278 ;EISSN: 1878-5808 ;DOI: 10.1016/S1359-0278(96)00061-2 ;PMID: 9080191

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13
Diversified Sequences of Peptide Epitope for Same-RNA Recognition
Diversified Sequences of Peptide Epitope for Same-RNA Recognition
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Diversified Sequences of Peptide Epitope for Same-RNA Recognition

Proceedings of the National Academy of Sciences - PNAS, 1993-11, Vol.90 (21), p.10046-10050 [Peer Reviewed Journal]

Copyright 1993 The National Academy of Sciences of the United States of America ;1994 INIST-CNRS ;Copyright National Academy of Sciences Nov 1, 1993 ;ISSN: 0027-8424 ;EISSN: 1091-6490 ;DOI: 10.1073/pnas.90.21.10046 ;PMID: 7694278 ;CODEN: PNASA6

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14
Long- and short-range interactions in native protein structures are consistent/minimally frustrated in sequence space
Long- and short-range interactions in native protein structures are consistent/minimally frustrated in sequence space
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Long- and short-range interactions in native protein structures are consistent/minimally frustrated in sequence space

Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted.

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15
Inverse Protein Folding
Inverse Protein Folding
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Inverse Protein Folding

APPROVED FOR PUBLIC RELEASE

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