Journal
APPLIED PHYSICS LETTERS
Volume 96, Issue 15, Pages -Publisher
AMER INST PHYSICS
DOI: 10.1063/1.3385388
Keywords
biomechanics; molecular biophysics; molecular configurations; molecular dynamics method; polymers; proteins
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Funding
- Office of Naval Research [N00014-08-1-00844]
- National Science Foundation
- National Science Foundation [TG-MSS090007]
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Spider silk is an ultrastrong and extensible self-assembling biopolymer that outperforms the mechanical characteristics of many synthetic materials including steel. Here we report atomic-level structures that represent aggregates of MaSp1 proteins from the N. Clavipes silk sequence based on a bottom-up computational approach using replica exchange molecular dynamics. We discover that poly-alanine regions predominantly form distinct and orderly beta-sheet crystal domains while disorderly structures are formed by poly-glycine repeats, resembling 3(1)-helices. These could be the molecular source of the large semicrystalline fraction observed in silks, and also form the basis of the so-called prestretched molecular configuration. Our structures are validated against experimental data based on dihedral angle pair calculations presented in Ramachandran plots, alpha-carbon atomic distances, as well as secondary structure content.
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