LightNobel: Improving Sequence Length Limitation in Protein Structure Prediction Model via Adaptive Activation Quantization
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arXiv
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| Format: | Preprint |
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2025
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| _version_ | 1866909607000014848 |
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| author | Han, Seunghee Choi, Soongyu Kim, Joo-Young |
| author_facet | Han, Seunghee Choi, Soongyu Kim, Joo-Young |
| contents | Recent advances in Protein Structure Prediction Models (PPMs), such as AlphaFold2 and ESMFold, have revolutionized computational biology by achieving unprecedented accuracy in predicting three-dimensional protein folding structures. However, these models face significant scalability challenges, particularly when processing proteins with long amino acid sequences (e.g., sequence length > 1,000). The primary bottleneck that arises from the exponential growth in activation sizes is driven by the unique data structure in PPM, which introduces an additional dimension that leads to substantial memory and computational demands. These limitations have hindered the effective scaling of PPM for real-world applications, such as analyzing large proteins or complex multimers with critical biological and pharmaceutical relevance.
In this paper, we present LightNobel, the first hardware-software co-designed accelerator developed to overcome scalability limitations on the sequence length in PPM. At the software level, we propose Token-wise Adaptive Activation Quantization (AAQ), which leverages unique token-wise characteristics, such as distogram patterns in PPM activations, to enable fine-grained quantization techniques without compromising accuracy. At the hardware level, LightNobel integrates the multi-precision reconfigurable matrix processing unit (RMPU) and versatile vector processing unit (VVPU) to enable the efficient execution of AAQ. Through these innovations, LightNobel achieves up to 8.44x, 8.41x speedup and 37.29x, 43.35x higher power efficiency over the latest NVIDIA A100 and H100 GPUs, respectively, while maintaining negligible accuracy loss. It also reduces the peak memory requirement up to 120.05x in PPM, enabling scalable processing for proteins with long sequences. |
| format | Preprint |
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arxiv_https___arxiv_org_abs_2505_05893 |
| institution | arXiv |
| publishDate | 2025 |
| record_format | arxiv |
| spellingShingle | LightNobel: Improving Sequence Length Limitation in Protein Structure Prediction Model via Adaptive Activation Quantization Han, Seunghee Choi, Soongyu Kim, Joo-Young Hardware Architecture Artificial Intelligence Emerging Technologies Machine Learning Biomolecules B.7; I.2; J.3 Recent advances in Protein Structure Prediction Models (PPMs), such as AlphaFold2 and ESMFold, have revolutionized computational biology by achieving unprecedented accuracy in predicting three-dimensional protein folding structures. However, these models face significant scalability challenges, particularly when processing proteins with long amino acid sequences (e.g., sequence length > 1,000). The primary bottleneck that arises from the exponential growth in activation sizes is driven by the unique data structure in PPM, which introduces an additional dimension that leads to substantial memory and computational demands. These limitations have hindered the effective scaling of PPM for real-world applications, such as analyzing large proteins or complex multimers with critical biological and pharmaceutical relevance. In this paper, we present LightNobel, the first hardware-software co-designed accelerator developed to overcome scalability limitations on the sequence length in PPM. At the software level, we propose Token-wise Adaptive Activation Quantization (AAQ), which leverages unique token-wise characteristics, such as distogram patterns in PPM activations, to enable fine-grained quantization techniques without compromising accuracy. At the hardware level, LightNobel integrates the multi-precision reconfigurable matrix processing unit (RMPU) and versatile vector processing unit (VVPU) to enable the efficient execution of AAQ. Through these innovations, LightNobel achieves up to 8.44x, 8.41x speedup and 37.29x, 43.35x higher power efficiency over the latest NVIDIA A100 and H100 GPUs, respectively, while maintaining negligible accuracy loss. It also reduces the peak memory requirement up to 120.05x in PPM, enabling scalable processing for proteins with long sequences. |
| title | LightNobel: Improving Sequence Length Limitation in Protein Structure Prediction Model via Adaptive Activation Quantization |
| topic | Hardware Architecture Artificial Intelligence Emerging Technologies Machine Learning Biomolecules B.7; I.2; J.3 |
| url | https://arxiv.org/abs/2505.05893 |