H
Heman Chao
Researcher at University of Alberta
Publications - 32
Citations - 1897
Heman Chao is an academic researcher from University of Alberta. The author has contributed to research in topics: Antifreeze protein & Ice binding. The author has an hindex of 17, co-authored 31 publications receiving 1822 citations. Previous affiliations of Heman Chao include Queen's University.
Papers
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Journal ArticleDOI
Structural basis for the binding of a globular antifreeze protein to ice
TL;DR: The 1.25 Å crystal structure of recombinant type III AFP (QAE iso-form9) from eel pout is reported, which reveals a remarkably flat amphipathic ice-binding site where five hydrogen-bonding atoms match two ranks of oxygens on the ice prism plane in the (0001) direction, giving high ice- binding affinity and specificity.
Journal ArticleDOI
A diminished role for hydrogen bonds in antifreeze protein binding to ice.
Heman Chao,Michael E. Houston,Robert S. Hodges,Cyril M. Kay,Brian D. Sykes,Michele C. Loewen,Peter L. Davies,Frank D. Sönnichsen +7 more
TL;DR: The results call into question the role of hydrogen bonds and suggest a much more significant role for entropic effects and van der Waals interactions in binding AFP to ice.
Journal ArticleDOI
New ice-binding face for type I antifreeze protein.
Jason Baardsnes,Leslie H. Kondejewski,Robert S. Hodges,Heman Chao,Cyril M. Kay,Peter L. Davies +5 more
TL;DR: This work proposes a new ice‐binding face for type I AFP that encompasses the conserved Ala‐rich surface and adjacent Thr, and investigates the role of Ala to Leu steric mutations around the helix.
Patent
Card-based biosensor device
TL;DR: In this article, a diagnostic card device for use in detecting or quantitating an analyte present in a liquid sample, comprising a card substrate having a sample introduction region, a biosensor, and a sample-flow pathway communicating between the sample-introduction region and the biosensor; and a signal responsive element for recording such signal.
Journal ArticleDOI
Structure‐function relationship in the globular type III antifreeze protein: Identification of a cluster of surface residues required for binding to ice
TL;DR: The results suggest that the C‐terminal β‐sheet of Type III AFP is primarily responsible for antifreeze activity, and they identify N14, T18, and Q44 as key residues for the AFP‐ice interaction.