Statistical analysis of protein structures suggests that buried ionizable residues in proteins are hydrogen bonded or form salt bridges

scientific article published on May 10, 2011

Statistical analysis of protein structures suggests that buried ionizable residues in proteins are hydrogen bonded or form salt bridges is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1002/PROT.23067
P953full work available at URLhttps://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.23067
https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.23067
P698PubMed publication ID21560169

P50authorGeorge I MakhatadzeQ88340910
P2093author name stringJeffrey Bush
P2860cites workProtein stability imposes limits on organism complexity and speed of molecular evolutionQ36092556
High tolerance for ionizable residues in the hydrophobic interior of proteinsQ36976733
Heat capacity changes upon burial of polar and nonpolar groups in proteinsQ38272583
Thermal adaptation of viruses and bacteriaQ39887443
Hydrogen bonding in globular proteinsQ40188265
Optimization of the electrostatic interactions between ionized groups and peptide dipoles in proteinsQ42845915
Hydrophobicity of amino acid subgroups in proteinsQ43537136
Swiss-PDB Viewer (Deep View).Q43683247
Thermodynamic consequences of burial of polar and non-polar amino acid residues in the protein interiorQ44038207
Are acidic and basic groups in buried proteins predicted to be ionized?Q46458086
Ion-pairs in proteinsQ47649652
Hydrophobic bonding and accessible surface area in proteinsQ47881268
Messages from ultrahigh resolution crystal structuresQ47993389
Prediction of electrostatic effects of engineering of protein chargesQ52584895
What about protein polarity?Q58977201
Calculation of electrostatic potentials in an enzyme active siteQ59067672
On the environment of ionizable groups in globular proteinsQ71303716
Tolerance to the substitution of buried apolar residues by charged residues in the homologous protein structuresQ79319216
Buried charged surface in proteinsQ27628399
Crystallographic Study of Hydration of an Internal Cavity in Engineered Proteins with Buried Polar or Ionizable GroupsQ27649489
Structural Bases for Stability–Function Tradeoffs in Antibiotic ResistanceQ27658160
A relationship between protein stability and protein functionQ27730341
The interpretation of protein structures: Estimation of static accessibilityQ27860750
Comparative protein modelling by satisfaction of spatial restraintsQ27860866
Satisfying hydrogen bonding potential in proteinsQ27860940
Close-range electrostatic interactions in proteinsQ28204004
PDB-REPRDB: a database of representative protein chains from the Protein Data Bank (PDB) in 2003.Q30332393
Molecular dynamics study of water penetration in staphylococcal nuclease.Q30350921
Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydrationQ30422341
Water penetration in the low and high pressure native states of ubiquitinQ33298524
How protein stability and new functions trade offQ33332450
Charges in the hydrophobic interior of proteinsQ34136707
Interior and surface of monomeric proteinsQ34187430
Conformational consequences of ionization of Lys, Asp, and Glu buried at position 66 in staphylococcal nucleaseQ36026093
P433issue7
P407language of work or nameEnglishQ1860
P921main subjectstatisticsQ12483
chemical modelQ25109595
P304page(s)2027-2032
P577publication date2011-05-10
P1433published inProteinsQ7251514
P1476titleStatistical analysis of protein structures suggests that buried ionizable residues in proteins are hydrogen bonded or form salt bridges
P478volume79

Reverse relations

cites work (P2860)
Q85248270A Buried Ionizable Residue Destabilizes the Native State and the Transition State in the Folding of Monellin
Q61806942Antiproliferative and Proapoptotic Effects of a Protein Component Purified from Dallas on Cancer Cells and
Q48769825Computational Studies of the Active and Inactive Regulatory Domains of Response Regulator PhoP Using Molecular Dynamics Simulations
Q47650790Isotope-Labeled Aspartate Sidechain as a Non-Perturbing Infrared Probe: Application to Investigate the Dynamics of a Carboxylate Buried Inside a Protein
Q37642482Molecular determinant of the effects of hydrostatic pressure on protein folding stability
Q42047273Peptide-lipid interactions of the stress-response peptide TisB that induces bacterial persistence
Q30373855ProteinVolume: calculating molecular van der Waals and void volumes in proteins.
Q37163190Protons as Second Messenger Regulators of G Protein Signaling
Q30155210Structural features of cholesteryl ester transfer protein: a molecular dynamics simulation study
Q37217194The role of cross-chain ionic interactions for the stability of collagen model peptides.

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