Protein structure prediction guided by crosslinking restraints--A systematic evaluation of the impact of the crosslinking spacer length.

ABSTRACT: Recent development of high-resolution mass spectrometry (MS) instruments enables chemical crosslinking (XL) to become a high-throughput method for obtaining structural information about proteins. Restraints derived from XL-MS experiments have been used successfully for structure refinement and protein-protein docking. However, one formidable question is under which circumstances XL-MS data might be sufficient to determine a protein's tertiary structure de novo? Answering this question will not only include understanding the impact of XL-MS data on sampling and scoring within a de novo protein structure prediction algorithm, it must also determine an optimal crosslinker type and length for protein structure determination. While a longer crosslinker will yield more restraints, the value of e

SUBMITTER: Hofmann T 

PROVIDER: S-EPMC4803439 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature