Environment and exposure to solvent of protein atoms. Lysozyme and insulin

1973/09/01 by Andrew Shrake, A. Shrake, J.A. Rupley · 8 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · #Biochemistry #Chemistry #Crystallization #Crystallography #Enzyme Structure and Function #Folding (DSP implementation) #Lysozyme #Mass Spectrometry Techniques and Applications #Molecule #Organic chemistry #Peptide #Protein Structure and Dynamics #Protein crystallization #Protein folding #Residue (chemistry) #Side chain #Solvent #Solvent exposure

paper · doi:10.1016/0022-2836(73)90011-9

crossref issued 1973/09/01 · crossref published 1973/09/01 · crossref published-print 1973/09/01 · openalex publication_date 1973/09/01 · crossref created 2005/02/10 · crossref deposited 2019/01/28 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/06 · crossref indexed 2026/08/06

Citations

• Atomic Positions in Rhombohedral 2-Zinc Insulin Crystals
• The interpretation of protein structures: Estimation of static accessibility
• van der Waals Volumes and Radii
• Tertiary Structure of Proteins. I. Representation and Computation of the Conformations

Cited by

• The nature of the accessible and buried surfaces in proteins
• The interpretation of protein structures: Total volume, group volume distributions and packing density
• Construction of new ligand binding sites in proteins of known structure
• Sheaf-theoretic representation of the proteolipid code
• The Effect of Hydration and Dynamics on the Mass Density of Single Proteins
• Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid.
• Scaling behaviour for the water transport in nanoconfined geometries
• Frederic M. Richards [wikipedia]