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Marc Hansen

dblp:162/7116 · DBLP profile ↗
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1ranked-venue papers
0as first author
0since 2021 · last 1999
—ORCID · none

Domains — the database's venue-derived domains; a paper can count in several

Applied, interdisciplinary, general and emerging computing · 1

Expertise — from the expertise taxonomy: the topics of the expert's papers under the CCF categories. A weight counts papers with recency: 1 for a paper about the topic, 0.3 when the topic is its context, halved every five years.

Interdisciplinary, comprehensive, and emerging computing
1 paper
Bioinformatics and computational biology · 100%

Topics — the 5 heaviest of 6, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology › protein structure prediction › template-based modeling
fold recognition
0.011999
DINAMO: interactive protein alignment and model building · Bioinform. 1999
Bioinformatics and computational biology › protein structure prediction › template-based modeling
homology modeling
0.011999
DINAMO: interactive protein alignment and model building · Bioinform. 1999
Bioinformatics and computational biology › protein sequence analysis
protein alignment
0.011999
DINAMO: interactive protein alignment and model building · Bioinform. 1999
Bioinformatics and computational biology
protein structure prediction
0.011999
DINAMO: interactive protein alignment and model building · Bioinform. 1999
Bioinformatics and computational biology › molecular informatics
molecular visualization
0.011999
DINAMO: interactive protein alignment and model building · Bioinform. 1999

Methods — techniques the papers use, named apart from their topics

multiple sequence alignment · 0.0dynamic programming · 0.0
YearPublicationVenuePosition
1999 DINAMO: interactive protein alignment and model building
abstract
MOTIVATION: To facilitate the process of structure prediction by both comparative modeling and fold recognition, we describe DINAMO, an interactive protein alignment building and model evaluation tool that dynamically couples a multiple sequence alignment editor to a molecular graphics display. DINAMO allows the user to optimize the alignment and model to satisfy the known heuristics of protein structure by means of a set of analysis tools. The analysis tools return information to both the alignment editor and graphics model in the form of visual cues (color, shape), allowing for rapid evaluation. Several analysis tools may be employed, including residue conservation, residue properties (charge, hydrophobicity, volume), residue environmental preference, and secondary structure propensity. RESULTS: We demonstrate DINAMO by building a model for submission in the 3rd annual Critical Assessment of Techniques for Protein Structure Prediction (CASP3) contest. AVAILABILITY: DINAMO is freely available as a local application or Web-based Java applet at http://tito.ucsc.edu/dinamo
Jesse Bentz, Albion Baucom, Marc Hansen, Lydia M. Gregoret
Bioinform.3