# Protein Allostery and Catalysis Beyond Bragg Diffraction

> **NIH NIH R35** · CORNELL UNIVERSITY · 2020 · $386,896

## Abstract

Abstract
What are the structural dynamics involved in protein allostery and catalysis? How do flexible enzymes perform
challenging chemistry? Can we animate crystal structures of proteins? These are outstanding questions in bi-
ology, which motivate studies of proteins in motion. Capturing proteins in action is the next frontier of structural
enzymology. By working at the interface of biochemistry and physical chemistry, we aim to go beyond the stat-
ic picture of enzymes that is obtained by traditional Bragg diffraction and instead recover dynamic information
with non-conventional X-ray scattering and diffraction approaches. We are particularly interested in enzymes of
biomedical importance that have been challenging to study by traditional methods, such as drug targets that
are allosterically regulated and enzymes that complex mechanisms to synthesize natural products with phar-
maceutical potential.

## Key facts

- **NIH application ID:** 9985910
- **Project number:** 5R35GM124847-04
- **Recipient organization:** CORNELL UNIVERSITY
- **Principal Investigator:** Nozomi Ando
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $386,896
- **Award type:** 5
- **Project period:** 2017-08-01 → 2022-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/9985910

## Citation

> US National Institutes of Health, RePORTER application 9985910, Protein Allostery and Catalysis Beyond Bragg Diffraction (5R35GM124847-04). Retrieved via AI Analytics 2026-05-25 from https://api.ai-analytics.org/grant/nih/9985910. Licensed CC0.

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