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Statistics of sequence-structure threading
scientific article published on April 1, 1995
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scholarly article
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Europe PubMed Central
PubMed publication ID
7648327
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21 June 2017
review article
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Europe PubMed Central
title
Statistics of sequence-structure threading
(English)
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Europe PubMed Central
PubMed publication ID
7648327
retrieved
21 June 2017
main subject
statistics
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author name string
S. H. Bryant
series ordinal
1
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Europe PubMed Central
PubMed publication ID
7648327
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A7648327
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14 July 2024
S. F. Altschul
series ordinal
2
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Europe PubMed Central
PubMed publication ID
7648327
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A7648327
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14 July 2024
language of work or name
English
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National Center for Biotechnology Information
PubMed publication ID
7648327
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publication date
1 April 1995
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7648327
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21 June 2017
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DOI
10.1016/0959-440X(95)80082-4
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https://api.elsevier.com/content/article/PII:0959440X95800824?httpAccept=text/plain
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10.1016/0959-440X(95)80082-4
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published in
Current Opinion in Structural Biology
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Europe PubMed Central
PubMed publication ID
7648327
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21 June 2017
volume
5
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Europe PubMed Central
PubMed publication ID
7648327
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21 June 2017
issue
2
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Europe PubMed Central
PubMed publication ID
7648327
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21 June 2017
page(s)
236-244
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Europe PubMed Central
PubMed publication ID
7648327
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21 June 2017
cites work
Statistical methods and insights for protein and DNA sequences
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10.1016/0959-440X(95)80082-4
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Issues in searching molecular sequence databases
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10.1016/0959-440X(95)80082-4
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Sensitive methods for determining the relatedness of proteins with limited sequence homology
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Catching a common fold
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10.1016/0959-440X(95)80082-4
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New programs for protein tertiary structure prediction
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De novo and inverse folding predictions of protein structure and dynamics
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Protein fold recognition
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Structure prediction of proteins--where are we now?
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Boltzmann's principle, knowledge-based mean fields and protein folding. An approach to the computational determination of protein structures
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The relation between the divergence of sequence and structure in proteins
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One thousand families for the molecular biologist
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Ancient conserved regions in new gene sequences and the protein databases
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A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure
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A new approach to protein fold recognition
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Topology fingerprint approach to the inverse protein folding problem
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An empirical energy function for threading protein sequence through the folding motif
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A proposed structural model of domain 1 of fasciclin III neural cell adhesion protein based on an inverse folding algorithm
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Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling
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Protein structural similarities predicted by a sequence-structure compatibility method
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Three-dimensional profiles from residue-pair preferences: identification of sequences with beta/alpha-barrel fold
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Improved tools for biological sequence comparison
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Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes
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Applications and statistics for multiple high-scoring segments in molecular sequences
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Maximum-likelihood estimation of the statistical distribution of Smith-Waterman local sequence similarity scores
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Rapid and accurate estimates of statistical significance for sequence data base searches
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Analysis of gene duplication repeats in the myosin rod.
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A general method applicable to the search for similarities in the amino acid sequence of two proteins
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On the Theory and Computation of Evolutionary Distances
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On the statistical assessment of similarities in DNA sequences
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Random sequences
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Recognition of distantly related proteins through energy calculations
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Contact potential that recognizes the correct folding of globular proteins
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Identification of protein folds: matching hydrophobicity patterns of sequence sets with solvent accessibility patterns of known structures
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Protein tertiary structure recognition using optimized Hamiltonians with local interactions
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Environment-specific amino acid substitution tables: tertiary templates and prediction of protein folds
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Alignment and searching for common protein folds using a data bank of structural templates
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A Structural Basis for Sequence Comparisons
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14 July 2024
Hamiltonians for protein tertiary structure prediction based on three-dimensional environment principles
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10.1016/0959-440X(95)80082-4
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Development of pseudoenergy potentials for assessing protein 3-D-1-D compatibility and detecting weak homologies
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Prediction of protein structure by evaluation of sequence-structure fitness. Aligning sequences to contact profiles derived from three-dimensional structures
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The three-dimensional profile method using residue preference as a continuous function of residue environment
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10.1016/0959-440X(95)80082-4
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Correctly folded proteins make twice as many hydrophobic contacts
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10.1016/0959-440X(95)80082-4
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14 July 2024
Identification of native protein folds amongst a large number of incorrect models. The calculation of low energy conformations from potentials of mean force
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10.1016/0959-440X(95)80082-4
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14 July 2024
Detection of native-like models for amino acid sequences of unknown three-dimensional structure in a data base of known protein conformations
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10.1016/0959-440X(95)80082-4
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14 July 2024
Recognition of errors in three-dimensional structures of proteins
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10.1016/0959-440X(95)80082-4
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14 July 2024
Factors influencing the ability of knowledge-based potentials to identify native sequence-structure matches
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10.1016/0959-440X(95)80082-4
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14 July 2024
Non-globular domains in protein sequences: automated segmentation using complexity measures
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10.1016/0959-440X(95)80082-4
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14 July 2024
De novo protein design using pairwise potentials and a genetic algorithm
series ordinal
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10.1016/0959-440X(95)80082-4
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14 July 2024
Empirical and structural models for insertions and deletions in the divergent evolution of proteins.
series ordinal
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10.1016/0959-440X(95)80082-4
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14 July 2024
Sequence alignment and penalty choice. Review of concepts, case studies and implications
series ordinal
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10.1016/0959-440X(95)80082-4
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14 July 2024
The frequency of ion-pair substructures in proteins is quantitatively related to electrostatic potential: a statistical model for nonbonded interactions
series ordinal
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DOI
10.1016/0959-440X(95)80082-4
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14 July 2024
Searching protein structure databases has come of age.
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10.1016/0959-440X(95)80082-4
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14 July 2024
Identifiers
DOI
10.1016/0959-440X(95)80082-4
1 reference
stated in
Europe PubMed Central
PubMed publication ID
7648327
retrieved
21 June 2017
PubMed publication ID
7648327
1 reference
stated in
Europe PubMed Central
PubMed publication ID
7648327
retrieved
21 June 2017
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