Antifreeze proteins (AFPs) are a family of ice-binding proteins found in aquatic life, insects, and microorganisms that live in areas where temperatures drop below zero degrees celsius . AFPs have an ice-binding face that inhibits the growth of ice crystals in vivo. This binding keeps ice crystals small enough to prevent cellular damage, thereby protecting the organism. Due to AFP's ability to specifically bind to ice crystals in a sea of liquid water, these proteins have become an important model system for understanding molecular recognition. The present study focuses on M1.1 AFP, a 7.1 kD type III AFP found in fish, such as arctic pout. By encapsulating the protein in a reverse micelle, comprehensive measurement of the water dynamics across the protein surface may be performed using nuclear magnetic resonance (NMR). Studying the movement of water near the ice-binding face is crucial for understanding the mechanism of action of these proteins. Such insight will inform development of real world applications, such as biocompatible additives to extend the lifespan of blood samples or protect transplant organs from environmental damage.