A two-component nucleation model of protein hydrophobicity

Journal of Theoretical Biology

Volumn 216, Issue 2, 2002, Pages 139-146

  Silverman, B David ^a  

^a IBM T J WATSON RESEARCH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLOBULAR PROTEIN;

HYDROPHOBICITY; PROTEIN;

AMINO ACID ANALYSIS; ARTICLE; CALCULATION; HYDROPHILICITY; HYDROPHOBICITY; MATHEMATICAL ANALYSIS; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE;

EID: 0036305289     PISSN: 00225193     EISSN: None     Source Type: Journal    
DOI: 10.1006/jtbi.2002.2553     Document Type: Article

References (19)

1. Polar residues in the protein core of Escherichia Coli thioredoxin are important for fold specificity
2. Polarity as a criterion in protein design
3. Improving the performance of Rosetta using multiple sequence alignment information and global measures of hydrophobic core formation
4. Hydrophobic moments and protein structure
5. Evaluation of protein models by atomic solvation preference
6. Effects of compact volume and chain stiffness on the conformations of native proteins
7. Recognizing native folds by the arrangement of hydrophobic and polar residues
8. Some factors in the interpretation of protein denaturation
9. A simple method for displaying the hydropathic character of a protein
10. Buried charged surface in proteins
11. A method for predicting nucleation sites for protein folding based on hydrophobic contacts
12. Empirical studies of hydrophobicity. 3. Radial distribution of clusters of hydrophobic and hydrophilic amino acids
13. Criteria that discriminate between native proteins and incorrectly folded models
14. Structure and function of haemoglobin
15. Hydrophobicity, hydrophilicity, and the radial and orientational distributions of residues in native proteins
16. Hydrophobic basis of packing of globular proteins
17. Hydrophobicity of amino acid residues in globular proteins
18. Hydrophobic moments of protein structures: Spatially profiling the distribution
19. Detecting native protein folds among large decoy sets with hydrophobic moment profiling