Molecular interactions in protein crystals: Solvent accessible surface and stability

Proteins: Structure, Function, and Bioinformatics

Volumn 8, Issue 1, 1990, Pages 1-5

  Islam, Suhail A ^a   Weaver, David L ^b  

^a IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

^b TUFTS UNIVERSITY   (United States)

Author keywords

accessible area; crystalline environment; dimeric proteins; hydrophobic interaction; linear correlation; monomeric proteins

Indexed keywords

ARTICLE; CRYSTAL; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE;

MOLECULAR WEIGHT; PROTEIN CONFORMATION; PROTEINS; SOLVENTS; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; SURFACE PROPERTIES; THERMODYNAMICS;

EID: 0025281494     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.340080103     Document Type: Article

References (15)

1. Structural invariants in protein folding
2. Surface area of globular proteins
3. Accessible area, packing volumes and interaction surfaces of globular proteins
4. Interior and surface of monomeric proteins
5. The accessible surface area and stability of ologomeric proteins
6. The surface area of monomeric proteins: Significance of power law behavior
7. Some factors in the interpretation of protein denaturation
8. Solvation energy in protein folding and binding
9. Protein folding dynamics
10. The Protein Data Bank: A computerarchival file for macromolecular structures
11. The interpretation of protein structures: Estimation of static accessibility
12. Solvent accessibility properties of complex proteins