# Ultrafast biological dynamics for protein properties and functions

> **NIH NIH R35** · OHIO STATE UNIVERSITY · 2020 · $204,000

## Abstract

Project Summary/Abstract
 Protein dynamics is essential for its biological function. With integration of molecular
biology, state-of-the-art time-resolved laser spectroscopy and computation simulations, the
biological dynamics now can be studied from the initial ultrafast motions to longtime
fluctuations on the most fundamental level. The molecular mechanisms thus can be revealed.
We have recently investigated the dynamics and mechanism of water-protein interactions and
elucidated the fundamental water-protein coupling motions occurring on the picosecond time
scales, an ideal timescale to bridge the gap between ultrafast bulk-water motions and slow
protein fluctuations. The understanding of biological water is significant to a variety of
biological activities such as protein-ligand/drug recognition and enzymatic catalysis. In another
direction, we also made significant advances on repair of UV-damaged DNA and mapped out
most repair processes in real time, including a series of ultrafast elementary reactions. We will
elucidate the complete repair photocycles at the local molecular level over a wide time scale
from femtoseconds to milliseconds and provide a molecular basis for potential applications
such as rational drug design for curing skin cancer. In this new effort, we will build a novel
time-resolved method to explore complex systems over a wide time range on two major areas
of (1) investigating interfacial water dynamics at protein-DNA and protein-protein complexes
to gain the deep understanding of binding properties and dynamic fluctuations of complexes
for biological functions and (2) examining two important photomachines of photoreceptors
(blue-light cryptochrome, UV-light receptor UVR8 and red-light phytochrome) and
photoenzyme photolyases. By systematic investigations of these dynamics over a wide time
range, we will uncover the entire process of initial signal transduction and reveal the reaction
mechanisms and photocycles of phytochrome and UVR8. The new knowledge obtained from
these efforts on biological-water dynamics and photoreceptor/photoenzymes photocycles is
significant to protein properties, dynamics, and functions involving protein-DNA/protein
complexes and signal transduction processes, and more importantly, is critical to practical
applications of drug design for a series of diseases such as mental disorder.

## Key facts

- **NIH application ID:** 10136754
- **Project number:** 3R35GM118332-05S1
- **Recipient organization:** OHIO STATE UNIVERSITY
- **Principal Investigator:** DONGPING ZHONG
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $204,000
- **Award type:** 3
- **Project period:** 2016-07-01 → 2022-01-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10136754

## Citation

> US National Institutes of Health, RePORTER application 10136754, Ultrafast biological dynamics for protein properties and functions (3R35GM118332-05S1). Retrieved via AI Analytics 2026-05-25 from https://api.ai-analytics.org/grant/nih/10136754. Licensed CC0.

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