Protein Design with Agent Rosetta: A Case Study for Specialized Scientific Agents
Authors: Jacopo Teneggi, S. M. Bargeen A. Turzo, Tanya Marwah, Alberto Bietti, P. Douglas Renfrew, Vikram Khipple Mulligan, Siavash Golkar
Organizations: Polymathic AI · Johns Hopkins University · Center for Computational Biology, Flatiron Institute · Google DeepMind (work was done while at the Simons Foundation) · Center for Computational Mathematics, Flatiron Institute · New York University
Large language models (LLMs) are capable of emulating reasoning and using tools, creating opportunities for autonomous agents that execute complex scientific tasks. Protein design provides a natural testbed: although machine learning (ML) methods achieve strong results, these are largely restricted to canonical amino acids and narrow objectives, leaving unfilled need for a generalist tool for broad design pipelines. We introduce Agent Rosetta, an LLM agent paired with a structured environment for operating Rosetta, the leading physics-based heteropolymer design software, capable of modeling non-canonical building blocks and geometries. Agent Rosetta iteratively refines designs to achieve user-defined objectives, combining LLM reasoning with Rosetta's generality. We evaluate Agent Rosetta on design with canonical amino acids, matching specialized models and expert baselines, and with non-canonical residues -- where ML approaches fail -- achieving comparable performance. Critically, prompt engineering alone often fails to generate Rosetta actions, demonstrating that environment design is essential for integrating LLM agents with specialized software. Our results show that properly designed environments enable LLM agents to make scientific software accessible while matching specialized tools and human experts.
Figures & tables
Relative absolute change (%)
Method
RMSD (Å)
Helix
Strand
Loop
Agent Rosetta (GPT-5)
2.6 (2.3/4.5)
2 (0/10)
3 (0/20)
13 (1/60)
Human baseline
3.1 (2.5/7.1)
3 (0/37)
8 (0/69)
22 (3/137)
Table 1: MD simulation results for the NCAA task. We report median (95% CI) across PDB structures, designs, and replicates.
Appendix figures & tables6 assets
Supplementary material from the paper’s appendix.
Appendix
Success rate (%)
Model
Task 1 (easy)
Task 2 (medium)
Task 3 (medium)
Task 4 (hard)
GPT-5
100
100
40
0
Gemini 2.5 Flash
90
10
0
0
Qwen3 235B Instruct (CoT)
90
20
0
0
Sonnet 4.5
90
100
90
0
Appendix
Table C.1 : Results of our environment ablation study where LLMs are instructed to generate parts of RosettaScripts XML scaffold usually automated by our environment. We average success rates over 10 independent query for each task.
9PL1
9VYW
9VYQ
9C14
Method
RMSD to init (mÅ)
pLDDT (0-100)
RMSD to init (mÅ)
pLDDT (0-100)
RMSD to init (mÅ)
pLDDT (0-100)
RMSD to init (mÅ)
pLDDT (0-100)
Qwen3 30B Instruct (CoT)
816 (+0/+46)
91.1 (-0.6/+0.2)
359 (-11/+29)
94.3 (-1.5/+0.2)
363 (-6/+21)
93.4 (-0.5/+1.5)
493 (+0/+90)
92.8 (-2.9/+0.0)
Qwen3 235B Instruct (CoT)
809 (-11/+15)
92.1 (-1.7/+0.1)
349 (-3/+24)
93.5 (-0.1/+0.2)
321 (-26/+14)
94.3 (-0.9/+0.2)
481 (-23/+30)
92.7 (-0.8/+1.4)
Gemini 2.5 Flash
758 (-11/+27)
92.5 (-2.4/+1.2)
324 (-17/+12)
94.1 (-0.2/+0.2)
306 (-16/+10)
94.4 (-0.5/+0.2)
421 (-14/+41)
94.0 (-1.3/+0.6)
GPT-5
732 (-5/+37)
91.4 (-1.5/+0.1)
351 (-4/+22)
92.9 (-0.2/+0.7)
326 (-9/+25)
94.5 (-0.8/+0.2)
489 (-36/+11)
93.8 (-1.8/+0.3)
Sonnet 4.5
788 (-16/+47)
91.8 (-0.5/+1.2)
341 (-26/+14)
94.4 (-1.4/+0.2)
305 (-1/+16)
94.3 (-0.3/+0.1)
462 (-23/+25)
92.4 (-0.7/+1.1)
Appendix
Table E.2 : Per-PDB results for all methods on fixed-backbone sequence design with canonical amino acids only. We report the best step-wise median and 95% confidence interval across 1000 bootstrap samples of 8 trajectories out of 16 independent trials per method. We select the best step in terms of the smallest 5 th percentile of the RMSD between the ESMFold predicted fold and the target conformation.
Method
RMSD to init (mÅ)
pLDDT (0-100)
Cost (USD)
Rosetta action success rate (%)
Fraction of reasoning tokens (%)
Gemini 2.5 Flash
571 ± 312
92.6 ± 2.6
0.126 ± 0.007
91 ± 3
93 ± 1
ProteinMPNN
581 ± 245
93.7 ± 2.5
na
na
na
GPT-5
608 ± 331
91.8 ± 2.9
0.329 ± 0.009
92 ± 2
69 ± 1
Qwen3 235B Instruct (CoT)
610 ± 319
92.4 ± 2.6
0.027 ± 0.003
86 ± 5
70 ± 3
Sonnet 4.5
620 ± 355
92.0 ± 3.1
0.669 ± 0.017
93 ± 1
64 ± 2
Random baseline
645 ± 353
91.2 ± 4.3
na
na
na
Appendix
Table E.3 : Summary of results across all 8 PDBs for all methods on fixed-backbone sequence design. We report mean and standard deviation of the best-of-8 median.
Figure F.1 : Comparison of the structure of tryptophan (TRP) and N1-formyl-tryptophan (TRF).
Method
Cost (USD)
Rosetta action success rate (%)
Fraction of reasoning tokens (%)
Rosetta RMSD to native (mÅ)
AF3 RMSD to native (mÅ)
AF3 pLDDT (0-100)
GPT-5
0.34 ± 0.03
84.0 ± 5.2
81.0 ± 1.2
162 ± 45
855 ± 526
82.2 ± 3.6
Gemini 2.5 Flash
0.15 ± 0.01
80.1 ± 7.5
88.1 ± 1.5
164 ± 41
1,137 ± 882
79.2 ± 4.7
Sonnet 4.5
0.70 ± 0.01
89.1 ± 4.0
65.2 ± 2.6
171 ± 45
1,766 ± 1,447
70.8 ± 11.2
Qwen3 235B Instruct (CoT)
0.03 ± 0.01
53.4 ± 22.9
71.0 ± 2.0
195 ± 70
3,133 ± 3,023
66.8 ± 19.3
Human baseline
na
na
na
201 ± 34
2,789 ± 3,574
78.6 ± 9.8
Appendix
Table F.4 : Summary of results across all 4 PDBs for all methods on inclusion of 1 TRF residue in the core of a given protein. We report mean and standard deviation of results in Table F.5 .
1QYS
6V67
Method
Rosetta RMSD (mÅ)
AF3 RMSD (mÅ)
AF3 pLDDT (0-100)
Rosetta RMSD (mÅ)
AF3 RMSD (mÅ)
AF3 pLDDT (0-100)
Qwen3 235B Instruct (CoT)
174 ± 4
627 ± 119
86.6 ± 4.0
111 ± 2
444 ± 189
79.0 ± 3.1
Gemini 2.5 Flash
170 ± 10
798 ± 677
85.9 ± 2.3
109 ± 2
347 ± 38
78.2 ± 0.8
GPT-5
166 ± 1
796 ± 81
84.6 ± 2.2
104 ± 2
374 ± 60
81.0 ± 1.7
Sonnet 4.5
157 ± 5
773 ± 252
82.3 ± 1.2
114 ± 3
604 ± 143
78.5 ± 1.6
Human baseline
182 ± 3
985 ± 158
84.8 ± 2.9
181 ± 6
476 ± 0
83.7 ± 0.0
Appendix
Table F.5 : Per-PDB results for all methods on inclusion of a TRF residue in the core of an input protein structure. For each method, we filter successful designs, and select the top 10 in order of increasing RMSD between the Rosetta Pose and the native PDB. We validate the fold of the selected designs with AF3, and report RMSD between the predicted fold and the native structure as well as pLDDT. We report average and standard deviation over the top 10 designs. The human baseline is marked as “na” for 8UZL because it fails to include any TRF residues.
State Key Lab. of Chemo & Biosensing, Coll. of Comp. Sci. & Electron. Eng., Hunan University · State Key Laboratory for Novel Software Technology, Sch. of Comput. Sci., Nanjing University · The Chinese University of Hong Kong +6