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English
Salt bridge interactions: stability of the ionic and neutral complexes in the gas phase, in solution, and in proteins.
scientific article published in July 1998
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Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 November 2019
title
Salt bridge interactions: stability of the ionic and neutral complexes in the gas phase, in solution, and in proteins
(English)
1 reference
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Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 November 2019
author
Xavier Barril
series ordinal
1
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Europe PubMed Central
PubMed publication ID
9672043
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13 November 2019
F. Javier Luque
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4
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Europe PubMed Central
PubMed publication ID
9672043
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
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13 November 2019
Modesto Orozco
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C Alemán
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2
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Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
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13 November 2019
M Orozco
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3
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Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
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language of work or name
English
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publication date
1 July 1998
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Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 November 2019
published in
Proteins
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 November 2019
volume
32
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 November 2019
issue
1
1 reference
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Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 November 2019
page(s)
67-79
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Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 November 2019
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Determinants of protein thermostability observed in the 1.9-A crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
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Energetic contribution of solvent-exposed ion pairs to alpha-helix structure
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Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase. Appendix: Kinetic analysis of dimeric enzymes that reversibly dissociate into inactive subunits
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21 January 2018
Conformational equilibria in -and -chymotrypsin. The energetics and importance of the salt bridge
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Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2
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Simulation of enzyme reactions using valence bond force fields and other hybrid quantum/classical approaches
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Identifiers
DOI
10.1002/(SICI)1097-0134(19980701)32:1<67::AID-PROT8>3.0.CO;2-B
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 November 2019
PubMed publication ID
9672043
1 reference
stated in
Europe PubMed Central
PubMed publication ID
9672043
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9672043%20AND%20SRC:MED&resulttype=core&format=json
retrieved
13 November 2019
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