A copy of this work was available on the public web and has been preserved in the Wayback Machine. The capture dates from 2020; you can also visit the original URL.
The file type is application/pdf
.
Conformational flexibility of N-glycans in solution studied by REMD simulations
2012
Biophysical Reviews
Protein-glycan recognition regulates a wide range of biological and pathogenic processes. Conformational diversity of glycans in solution is apparently incompatible with specific binding to their receptor proteins. One possibility is that among the different conformational states of a glycan, only one conformer is utilized for specific binding to a protein. However, the labile nature of glycans makes characterizing their conformational states a challenging issue. All-atom molecular dynamics
doi:10.1007/s12551-012-0090-y
pmid:28510079
pmcid:PMC5418406
fatcat:nhecagstabhdfgplb7te3chedu