Issue 18, 2017

Conformational and hydration properties modulate ice recognition by type I antifreeze protein and its mutants

Abstract

The mechanism of ice recognition by antifreeze protein (AFP) is a topic of recent interest. Here, using equilibrium simulations and free energy calculations, we provide structural rationale to the observed experimental anomalies on type I AFP (wfAFP isoform HPLC6) and its mutants as well as probe the molecular origin of ice recognition by them. Our results clearly demonstrate that the interplay between the conformational and hydration properties dictates the ice binding ability of type I AFP and its mutants. We find that HPLC6 exists as a highly stable long helix which adsorbs on the ice surface through the ordered water cages around the CH3 group of threonine (THR) residues, rather than directly binding to the ice surface via threonine (THR) through hydrogen bonding. Upon mutating THR with serine (SER), the straight helix conformation of HPLC6 disappears and the most stable conformation is a kinked helix devoid of ice binding ability. Free energy calculations reveal that there is a dynamic equilibrium between straight and bent helical conformations in the case of a valine (VAL) mutant. The straight long helical form of the VAL mutant also has the ability to form an ordered water cage structure around the CH3 groups of the VAL residues and thereby efficiently adsorbs on an ice plane similar to the wild type AFP.

Graphical abstract: Conformational and hydration properties modulate ice recognition by type I antifreeze protein and its mutants

Supplementary files

Article information

Article type
Paper
Submitted
11 Jan 2017
Accepted
12 Apr 2017
First published
12 Apr 2017

Phys. Chem. Chem. Phys., 2017,19, 11678-11689

Conformational and hydration properties modulate ice recognition by type I antifreeze protein and its mutants

S. Chakraborty and B. Jana, Phys. Chem. Chem. Phys., 2017, 19, 11678 DOI: 10.1039/C7CP00221A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements