Identifying proteins of high designability via surface-exposure patterns

Proteins: Structure, Function and Genetics

Volumn 47, Issue 3, 2002, Pages 295-304

  Emberly, Eldon G ^a   Miller, Jonathan ^a   Zeng, Chen ^b   Wingreen, Ned S ^a   Tang, Chao ^a  

^a NEC LABORATORIES AMERICA   (United States)

^b GEORGE WASHINGTON UNIVERSITY   (United States)

Author keywords

Hydrophobicity; Off lattice model; Protein design; Protein structure prediction

Indexed keywords

POLYPEPTIDE;

ARTICLE; CONFORMATION; ENERGY; HYDROPHOBICITY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE ANALYSIS;

HYDROPHOBICITY; MODELS, MOLECULAR; PEPTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEINS;

EID: 0037093651     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10067     Document Type: Article

References (30)

1. Principles that govern the folding of protein chains
2. Proteins - 1000 Families for the molecular biologist
3. Protein superfamilies and domain superfolds
4. Population statistics of protein structures: Lessons from structural classifications
5. Estimating the total number of protein folds
6. Why do globular proteins fit the limited set of folding patterns?
7. Forces of tertiary structural organization in globular proteins
8. Searching for foldable protein structures using optimized energy functions
9. Emergence of preferred structures in a simple-model of protein-folding
10. Are protein folds atypical?
11. Designability, thermodynamic stability, and dynamics in protein folding: A lattice model study
12. Modeling evolutionary landscapes: Mutational stability, topology, and superfunnels in sequence space
13. A lattice statistical mechanics model of the conformational and sequence spaces of proteins
14. The effects of internal constraints on the configurations of chain molecules
15. Enumeration of all compact conformations of copolymers with random sequence of links
16. Minimum energy compact structures of random sequences of heteropolymers
17. Enumerations of the Hamiltonian walks on a cubic sublattice
18. The complexity and accuracy of discrete state models of protein structure
19. Some factors in the interpretation of protein denaturization
20. Dominant forces in protein folding
21. Nature of driving force for protein folding: A result from analyzing the statistical potential
22. The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions
23. Simplified representation of protein conformations for rapid simulation of protein folding
24. Hydrophilicity of polar amino acid side-chains is markedly reduced by flanking peptide bonds
25. Solvation energy in protein folding and binding
26. Surveying determinants of protein structure designability across different energy models and amino-acid alphabets: A consensus
27. Polymer principles of protein calorimetric two-state cooperativity