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Intrinsic protein electric fields: basic non-covalent interactions and relationship to protein-induced Stark effects
scientific article published on 01 August 1998
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Europe PubMed Central
PubMed publication ID
9733989
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9733989%20AND%20SRC:MED&resulttype=core&format=json
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3 December 2019
review article
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title
Intrinsic protein electric fields: basic non-covalent interactions and relationship to protein-induced Stark effects
(English)
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Europe PubMed Central
PubMed publication ID
9733989
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M Laberge
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1
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Europe PubMed Central
PubMed publication ID
9733989
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publication date
1 August 1998
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PubMed publication ID
9733989
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published in
Biochimica et Biophysica Acta
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PubMed publication ID
9733989
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1386
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Europe PubMed Central
PubMed publication ID
9733989
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2
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Europe PubMed Central
PubMed publication ID
9733989
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305-330
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Europe PubMed Central
PubMed publication ID
9733989
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3 December 2019
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Long-range surface charge-charge interactions in proteins. Comparison of experimental results with calculations from a theoretical method.
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Theoretical studies of enzymic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
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Stark spectroscopy: applications in chemistry, biology, and materials science
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A test of the role of electrostatic interactions in determining the CO stretch frequency in carbonmonoxymyoglobin
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Crystal structure of horseradish peroxidase C at 2.15 A resolution
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Structural determinants of the stretching frequency of CO bound to myoglobin
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Distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of three distal mutants
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Distal and proximal ligand interactions in heme proteins: correlations between C-O and Fe-C vibrational frequencies, oxygen-17 and carbon-13 nuclear magnetic resonance chemical shifts, and oxygen-17 nuclear quadrupole coupling constants in C17O- and
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Surface of cytochrome c: infrared spectroscopy of carboxyl groups
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Effect of charge interactions on the carboxylate vibrational stretching frequency in c-type cytochromes investigated by continuum electrostatic calculations and FTIR spectroscopy
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High-resolution three-dimensional structure of horse heart cytochrome c
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The Protein Data Bank. A computer-based archival file for macromolecular structures
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Refined crystal structure of calcium-liganded carp parvalbumin 4.25 at 1.5-A resolution
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Conformational effects of calcium release from parvalbumin: comparison of computational simulations with spectroscopic investigations
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Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale
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The structure of calf liver cytochrome b 5 at 2.8 A resolution
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7 January 2021
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Identifiers
DOI
10.1016/S0167-4838(98)00100-9
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9733989
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9733989%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 December 2019
PubMed publication ID
9733989
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9733989
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9733989%20AND%20SRC:MED&resulttype=core&format=json
retrieved
3 December 2019
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