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Namrata Anand

dblp:231/7667 · DBLP profile ↗
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1ranked-venue papers
1as first author
0since 2021 · last 2018
—ORCID · none

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

Artificial intelligence and machine learning · 1 · 1 first-author

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.

Artificial intelligence
1 paper
Generative modeling · 100%
Interdisciplinary, comprehensive, and emerging computing
1 paper
Bioinformatics and computational biology · 100%

Topics — the 4 heaviest of 4, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Machine learning › Generative modeling
generative adversarial network
0.312018
Generative modeling for protein structures · NeurIPS 2018
Machine learning › Generative modeling › protein design
protein structure generation
0.312018
Generative modeling for protein structures · NeurIPS 2018
Bioinformatics and computational biology › structural bioinformatics
protein structure
0.312018
Generative modeling for protein structures · NeurIPS 2018
Bioinformatics and computational biology › protein design
protein structure generation
0.312018
Generative modeling for protein structures · NeurIPS 2018

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

generative adversarial network · 0.7convex optimization · 0.7alternating direction method of multipliers · 0.7
YearPublicationVenuePosition
2018 Generative modeling for protein structures
abstract
Analyzing the structure and function of proteins is a key part of understanding biology at the molecular and cellular level. In addition, a major engineering challenge is to design new proteins in a principled and methodical way. Current computational modeling methods for protein design are slow and often require human oversight and intervention. Here, we apply Generative Adversarial Networks (GANs) to the task of generating protein structures, toward application in fast de novo protein design. We encode protein structures in terms of pairwise distances between alpha-carbons on the protein backbone, which eliminates the need for the generative model to learn translational and rotational symmetries. We then introduce a convex formulation of corruption-robust 3D structure recovery to fold the protein structures from generated pairwise distance maps, and solve these problems using the Alternating Direction Method of Multipliers. We test the effectiveness of our models by predicting completions of corrupted protein structures and show that the method is capable of quickly producing structurally plausible solutions.
Namrata Anand, Po-Ssu Huang
NeurIPS1