Biophysical Characteristics of Cholera Toxin and Escherichia coli Heat-Labile Enterotoxin Structure and Chemistry Lead to Differential Toxicity
The biophysical chemistry of macromolecular complexes confer their functional characteristics. We investigate the mechanisms that make the AB5 holotoxin of Vibrio cholerae (CT) a significantly more pathogenic molecule than the enterotoxin of Escherichia coli (LT) with which it shares 88% similarity...
Saved in:
Published in | The journal of physical chemistry. B Vol. 119; no. 3; pp. 1048 - 1061 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
22.01.2015
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | The biophysical chemistry of macromolecular complexes confer their functional characteristics. We investigate the mechanisms that make the AB5 holotoxin of Vibrio cholerae (CT) a significantly more pathogenic molecule than the enterotoxin of Escherichia coli (LT) with which it shares 88% similarity and whose structure is homologous with a backbone RMSD of 0.84 Å and imposes its deleterious effects though the same process to constitutively ADP-ribosylate adenylate cyclase. We present computational data that characterizes the impact of amino acid variations in the A2 tail, which helps to explain experimental data that demonstrate CT’s higher toxicity. A hydrophobic patch on the B pentamer interface and its interactions with the A subdomain are partially disrupted by the substitution of an aspartic acid (LT) for glycine in CT. CT’s holotoxin has less solvent accessible surface area (94 Å2 vs 54 Å2) and higher contact area (280 Å2 vs 241 Å2) with S228, which is a gatekeeper, partially controlling the diffusion of water into the pore. CT excludes water from the top of the central pore whereas LT allows much more water to interact. These biophysical properties of the toxins lead to their differential toxicity and resulting impact to human health. |
---|---|
AbstractList | The biophysical chemistry of macromolecular complexes confer their functional characteristics. We investigate the mechanisms that make the AB5 holotoxin of Vibrio cholerae (CT) a significantly more pathogenic molecule than the enterotoxin of Escherichia coli (LT) with which it shares 88% similarity and whose structure is homologous with a backbone RMSD of 0.84 Aa and imposes its deleterious effects though the same process to constitutively ADP-ribosylate adenylate cyclase. We present computational data that characterizes the impact of amino acid variations in the A2 tail, which helps to explain experimental data that demonstrate CT's higher toxicity. A hydrophobic patch on the B pentamer interface and its interactions with the A subdomain are partially disrupted by the substitution of an aspartic acid (LT) for glycine in CT. CT's holotoxin has less solvent accessible surface area (94 Aa super(2) vs 54 Aa super(2)) and higher contact area (280 Aa super(2) vs 241 Aa super(2)) with S228, which is a gatekeeper, partially controlling the diffusion of water into the pore. CT excludes water from the top of the central pore whereas LT allows much more water to interact. These biophysical properties of the toxins lead to their differential toxicity and resulting impact to human health. The biophysical chemistry of macromolecular complexes confer their functional characteristics. We investigate the mechanisms that make the AB5 holotoxin of Vibrio cholerae (CT) a significantly more pathogenic molecule than the enterotoxin of Escherichia coli (LT) with which it shares 88% similarity and whose structure is homologous with a backbone RMSD of 0.84 Å and imposes its deleterious effects though the same process to constitutively ADP-ribosylate adenylate cyclase. We present computational data that characterizes the impact of amino acid variations in the A2 tail, which helps to explain experimental data that demonstrate CT's higher toxicity. A hydrophobic patch on the B pentamer interface and its interactions with the A subdomain are partially disrupted by the substitution of an aspartic acid (LT) for glycine in CT. CT's holotoxin has less solvent accessible surface area (94 Å(2) vs 54 Å(2)) and higher contact area (280 Å(2) vs 241 Å(2)) with S228, which is a gatekeeper, partially controlling the diffusion of water into the pore. CT excludes water from the top of the central pore whereas LT allows much more water to interact. These biophysical properties of the toxins lead to their differential toxicity and resulting impact to human health. The biophysical chemistry of macromolecular complexes confer their functional characteristics. We investigate the mechanisms that make the AB5 holotoxin of Vibrio cholerae (CT) a significantly more pathogenic molecule than the enterotoxin of Escherichia coli (LT) with which it shares 88% similarity and whose structure is homologous with a backbone RMSD of 0.84 Å and imposes its deleterious effects though the same process to constitutively ADP-ribosylate adenylate cyclase. We present computational data that characterizes the impact of amino acid variations in the A2 tail, which helps to explain experimental data that demonstrate CT’s higher toxicity. A hydrophobic patch on the B pentamer interface and its interactions with the A subdomain are partially disrupted by the substitution of an aspartic acid (LT) for glycine in CT. CT’s holotoxin has less solvent accessible surface area (94 Å2 vs 54 Å2) and higher contact area (280 Å2 vs 241 Å2) with S228, which is a gatekeeper, partially controlling the diffusion of water into the pore. CT excludes water from the top of the central pore whereas LT allows much more water to interact. These biophysical properties of the toxins lead to their differential toxicity and resulting impact to human health. |
Author | Shen, Tsai-wei Briggs, James M Brier, Lindsey M Craft, John W |
AuthorAffiliation | University of Houston Department of Biology and Biochemistry |
AuthorAffiliation_xml | – name: Department of Biology and Biochemistry – name: University of Houston |
Author_xml | – sequence: 1 givenname: John W surname: Craft fullname: Craft, John W – sequence: 2 givenname: Tsai-wei surname: Shen fullname: Shen, Tsai-wei – sequence: 3 givenname: Lindsey M surname: Brier fullname: Brier, Lindsey M – sequence: 4 givenname: James M surname: Briggs fullname: Briggs, James M email: jbriggs@uh.edu |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/25322200$$D View this record in MEDLINE/PubMed |
BookMark | eNqFkc-O0zAQhy20iP0DB14A-YIEh8DYaZzkCKWwSJU4sJyjyWSsuErjYjsSfQpeGe-27AmJg2Vr9M1nj3_X4mL2MwvxUsE7BVq93x0qMBW09ERcqUpDkVd9cT4bBeZSXMe4A9CVbswzcamrUmsNcCV-f3T-MB6jI5zkesSAlDi4mBxF6W0u-YkDyjv_y80S50FuIo2ZoNGhJD85ecuYii32bmK5mXO3Tw_w9xQWSkvgh7b1yPusDUe5ZRxk8vKTs5YDz8nlq-_95NLxuXhqcYr84rzfiB-fN3fr22L77cvX9YdtgWWjUlGpltBiQyvQ7arEvmVr9FDBYLgsS2uBuB_6pm6bOg9b2sH2aGokIEu6HMob8ebkPQT_c-GYuvw64mnCmf0SO1UbDcbUSv8fNQZWAEa3GX17Qin4GAPb7hDcHsOxU9DdR9U9RpXZV2ft0u95eCT_ZpOB1ycAKXY7v4Q5f8g_RH8ASWKe1g |
CitedBy_id | crossref_primary_10_3389_fimmu_2020_575085 crossref_primary_10_1515_chem_2016_0021 crossref_primary_10_3103_S0891416821050049 crossref_primary_10_1038_s41598_018_30910_y crossref_primary_10_1038_s41598_021_03939_9 crossref_primary_10_3390_pharmaceutics14081671 crossref_primary_10_1016_j_cellsig_2022_110489 |
Cites_doi | 10.1016/0263-7855(96)00018-5 10.3390/biom3040997 10.1063/1.470117 10.1016/0021-9991(77)90098-5 10.1074/jbc.274.7.3962 10.1107/S0021889883010985 10.1006/jmbi.1993.1209 10.1002/elps.1150181505 10.1073/pnas.011442598 10.1083/jcb.148.6.1203 10.1002/(SICI)1096-987X(19961115)17:14<1633::AID-JCC5>3.0.CO;2-M 10.1006/jmbi.1994.1301 10.1002/jcc.540040211 10.1016/0005-2795(72)90265-6 10.1021/bi0360152 10.3390/toxins2030310 10.1128/mr.60.1.167-215.1996 10.1128/IAI.71.7.4093-4101.2003 10.1083/jcb.200207120 10.1006/jmbi.1995.0456 10.1016/0010-4655(95)00043-F 10.1016/S0092-8674(01)00289-6 10.1063/1.445869 10.1016/j.jmb.2007.12.075 10.1152/ajpgi.2001.280.5.G781 10.1002/jcc.20289 10.1016/j.tibs.2003.10.002 10.1074/jbc.272.24.15562 10.1021/jp973084f 10.1002/jcc.21287 |
ContentType | Journal Article |
Copyright | Copyright © 2014 American Chemical
Society |
Copyright_xml | – notice: Copyright © 2014 American Chemical Society |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QL 7T2 7U2 C1K 7SR 7U5 8BQ 8FD JG9 L7M |
DOI | 10.1021/jp506509c |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Bacteriology Abstracts (Microbiology B) Health and Safety Science Abstracts (Full archive) Safety Science and Risk Environmental Sciences and Pollution Management Engineered Materials Abstracts Solid State and Superconductivity Abstracts METADEX Technology Research Database Materials Research Database Advanced Technologies Database with Aerospace |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Health & Safety Science Abstracts Safety Science and Risk Bacteriology Abstracts (Microbiology B) Environmental Sciences and Pollution Management Materials Research Database Engineered Materials Abstracts Solid State and Superconductivity Abstracts Technology Research Database Advanced Technologies Database with Aerospace METADEX |
DatabaseTitleList | Materials Research Database MEDLINE Health & Safety Science Abstracts |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Chemistry |
EISSN | 1520-5207 |
EndPage | 1061 |
ExternalDocumentID | 10_1021_jp506509c 25322200 b922454222 |
Genre | Journal Article |
GroupedDBID | - .K2 02 123 29L 4.4 53G 55A 5VS 7~N 85S 8RP AABXI ABFLS ABMVS ABPTK ABUCX ACGFS ACNCT ACS AEESW AENEX AFEFF ALMA_UNASSIGNED_HOLDINGS AQSVZ BAANH CS3 DU5 EBS ED ED~ EJD F20 F5P GNL IH9 IHE JG JG~ K2 LG6 PZZ RNS ROL TAE TN5 UI2 UKR UPT VF5 VG9 VQA W1F WH7 X YZZ ZGI ZHY --- -~X .DC AAHBH ABJNI ABQRX ACBEA ADHLV AHGAQ CGR CUPRZ CUY CVF ECM EIF GGK NPM XSW YQT ~02 AAYXX CITATION 7QL 7T2 7U2 C1K 7SR 7U5 8BQ 8FD JG9 L7M |
ID | FETCH-LOGICAL-a381t-519cafa8c402943ab9ef62d50d6e333ff0cebdb879872533fdfba67ac0cfc23d3 |
IEDL.DBID | ACS |
ISSN | 1520-6106 |
IngestDate | Fri Aug 16 14:39:59 EDT 2024 Fri Aug 16 21:11:41 EDT 2024 Fri Dec 06 01:33:48 EST 2024 Sat Sep 28 07:56:55 EDT 2024 Thu Aug 27 13:42:35 EDT 2020 |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 3 |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-a381t-519cafa8c402943ab9ef62d50d6e333ff0cebdb879872533fdfba67ac0cfc23d3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
PMID | 25322200 |
PQID | 1660400629 |
PQPubID | 23462 |
PageCount | 14 |
ParticipantIDs | proquest_miscellaneous_1762066712 proquest_miscellaneous_1660400629 crossref_primary_10_1021_jp506509c pubmed_primary_25322200 acs_journals_10_1021_jp506509c |
ProviderPackageCode | JG~ 55A AABXI GNL VF5 7~N VG9 W1F ACS AEESW AFEFF .K2 ABMVS ABUCX IH9 BAANH AQSVZ ED~ UI2 |
PublicationCentury | 2000 |
PublicationDate | 20150122 2015-Jan-22 2015-01-22 |
PublicationDateYYYYMMDD | 2015-01-22 |
PublicationDate_xml | – month: 01 year: 2015 text: 20150122 day: 22 |
PublicationDecade | 2010 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | The journal of physical chemistry. B |
PublicationTitleAlternate | J. Phys. Chem. B |
PublicationYear | 2015 |
Publisher | American Chemical Society |
Publisher_xml | – name: American Chemical Society |
References | Tsai B. (ref12/cit12) 2001; 104 Sixma T. K. (ref6/cit6) 1993; 230 Wernick N. L. B. (ref9/cit9) 2010; 2 Antosiewicz J. (ref23/cit23) 1994; 238 Ampapathi R. S. (ref16/cit16) 2008; 377 O’Neal C. J. (ref4/cit4) 2004; 43 Sears C. L. (ref5/cit5) 1996; 60 Jorgensen W. L. (ref27/cit27) 1983; 79 Zhang R. G. (ref2/cit2) 1995; 251 Lencer W. I. (ref7/cit7) 2001; 280 MacKerell A. D. (ref19/cit19) 1998; 102 Humphrey W. (ref26/cit26) 1996; 14 Lencer W. I. (ref10/cit10) 1997; 272 Rodighiero C. (ref15/cit15) 1999; 274 Lencer W. I. (ref11/cit11) 2003; 28 Essmann U. (ref28/cit28) 1995; 103 Tsai B. (ref13/cit13) 2002; 159 Guex N. (ref20/cit20) 1997; 18 Lospalluto J. J. (ref1/cit1) 1972; 257 Brooks B. R. (ref22/cit22) 2009; 30 Brooks B. (ref21/cit21) 1983; 4 Antosiewicz J. (ref24/cit24) 1996; 17 Teter K. (ref8/cit8) 2013; 3 Jobling M. G. (ref3/cit3) 2000; 97 Schmitz A. (ref14/cit14) 2000; 148 Connolly M. (ref30/cit30) 1983; 16 Madura J. D. (ref25/cit25) 1995; 91 Phillips J. C. (ref18/cit18) 2005; 26 Ryckaert J.-P. (ref29/cit29) 1977; 23 Tinker J. K. (ref17/cit17) 2003; 71 |
References_xml | – volume: 14 start-page: 33 year: 1996 ident: ref26/cit26 publication-title: J. Mol. Graph. doi: 10.1016/0263-7855(96)00018-5 contributor: fullname: Humphrey W. – volume: 3 start-page: 997 year: 2013 ident: ref8/cit8 publication-title: Biomolecules doi: 10.3390/biom3040997 contributor: fullname: Teter K. – volume: 103 start-page: 8577 year: 1995 ident: ref28/cit28 publication-title: J. Chem. Phys. doi: 10.1063/1.470117 contributor: fullname: Essmann U. – volume: 23 start-page: 327 year: 1977 ident: ref29/cit29 publication-title: J. Comput. Phys. doi: 10.1016/0021-9991(77)90098-5 contributor: fullname: Ryckaert J.-P. – volume: 274 start-page: 3962 year: 1999 ident: ref15/cit15 publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.7.3962 contributor: fullname: Rodighiero C. – volume: 16 start-page: 548 year: 1983 ident: ref30/cit30 publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889883010985 contributor: fullname: Connolly M. – volume: 230 start-page: 890 year: 1993 ident: ref6/cit6 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1993.1209 contributor: fullname: Sixma T. K. – volume: 18 start-page: 2714 year: 1997 ident: ref20/cit20 publication-title: Electrophoresis doi: 10.1002/elps.1150181505 contributor: fullname: Guex N. – volume: 97 start-page: 14662 year: 2000 ident: ref3/cit3 publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.011442598 contributor: fullname: Jobling M. G. – volume: 148 start-page: 1203 year: 2000 ident: ref14/cit14 publication-title: J. Cell. Biol. doi: 10.1083/jcb.148.6.1203 contributor: fullname: Schmitz A. – volume: 17 start-page: 1633 year: 1996 ident: ref24/cit24 publication-title: J. Comput. Chem. doi: 10.1002/(SICI)1096-987X(19961115)17:14<1633::AID-JCC5>3.0.CO;2-M contributor: fullname: Antosiewicz J. – volume: 238 start-page: 415 year: 1994 ident: ref23/cit23 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1994.1301 contributor: fullname: Antosiewicz J. – volume: 4 start-page: 187 year: 1983 ident: ref21/cit21 publication-title: J. Comput. Chem. doi: 10.1002/jcc.540040211 contributor: fullname: Brooks B. – volume: 257 start-page: 158 year: 1972 ident: ref1/cit1 publication-title: Biochim. Biophys. Acta doi: 10.1016/0005-2795(72)90265-6 contributor: fullname: Lospalluto J. J. – volume: 43 start-page: 3772 year: 2004 ident: ref4/cit4 publication-title: Biochemistry doi: 10.1021/bi0360152 contributor: fullname: O’Neal C. J. – volume: 2 start-page: 310 year: 2010 ident: ref9/cit9 publication-title: Toxins doi: 10.3390/toxins2030310 contributor: fullname: Wernick N. L. B. – volume: 60 start-page: 167 year: 1996 ident: ref5/cit5 publication-title: Microbiol. Rev. doi: 10.1128/mr.60.1.167-215.1996 contributor: fullname: Sears C. L. – volume: 71 start-page: 4093 year: 2003 ident: ref17/cit17 publication-title: Infect. Immun. doi: 10.1128/IAI.71.7.4093-4101.2003 contributor: fullname: Tinker J. K. – volume: 159 start-page: 207 year: 2002 ident: ref13/cit13 publication-title: J. Cell. Biol. doi: 10.1083/jcb.200207120 contributor: fullname: Tsai B. – volume: 251 start-page: 563 year: 1995 ident: ref2/cit2 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1995.0456 contributor: fullname: Zhang R. G. – volume: 91 start-page: 57 year: 1995 ident: ref25/cit25 publication-title: Comput. Phys. Commun. doi: 10.1016/0010-4655(95)00043-F contributor: fullname: Madura J. D. – volume: 104 start-page: 937 year: 2001 ident: ref12/cit12 publication-title: Cell doi: 10.1016/S0092-8674(01)00289-6 contributor: fullname: Tsai B. – volume: 79 start-page: 926 year: 1983 ident: ref27/cit27 publication-title: J. Chem. Phys. doi: 10.1063/1.445869 contributor: fullname: Jorgensen W. L. – volume: 377 start-page: 748 year: 2008 ident: ref16/cit16 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.12.075 contributor: fullname: Ampapathi R. S. – volume: 280 start-page: G781 year: 2001 ident: ref7/cit7 publication-title: Am. J. Physiol. Gastrointest. Liver. Physiol. doi: 10.1152/ajpgi.2001.280.5.G781 contributor: fullname: Lencer W. I. – volume: 26 start-page: 1781 year: 2005 ident: ref18/cit18 publication-title: J. Comput. Chem. doi: 10.1002/jcc.20289 contributor: fullname: Phillips J. C. – volume: 28 start-page: 639 year: 2003 ident: ref11/cit11 publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2003.10.002 contributor: fullname: Lencer W. I. – volume: 272 start-page: 15562 year: 1997 ident: ref10/cit10 publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.24.15562 contributor: fullname: Lencer W. I. – volume: 102 start-page: 3586 year: 1998 ident: ref19/cit19 publication-title: J. Phys. Chem. B doi: 10.1021/jp973084f contributor: fullname: MacKerell A. D. – volume: 30 start-page: 1545 year: 2009 ident: ref22/cit22 publication-title: J. Comput. Chem. doi: 10.1002/jcc.21287 contributor: fullname: Brooks B. R. |
SSID | ssj0025286 |
Score | 2.2539148 |
Snippet | The biophysical chemistry of macromolecular complexes confer their functional characteristics. We investigate the mechanisms that make the AB5 holotoxin of... |
SourceID | proquest crossref pubmed acs |
SourceType | Aggregation Database Index Database Publisher |
StartPage | 1048 |
SubjectTerms | Amino acids Aspartic acid Backbone Biophysical Phenomena Cholera Toxin - chemistry Cholera Toxin - metabolism Cholera Toxin - toxicity Escherichia coli Hot Temperature Hydrogen Bonding Molecular Dynamics Simulation Porosity Protein Conformation Similarity Solvents - chemistry Structure-Activity Relationship Surface Properties Toxicity Toxins Vibrio cholerae Water - chemistry |
Title | Biophysical Characteristics of Cholera Toxin and Escherichia coli Heat-Labile Enterotoxin Structure and Chemistry Lead to Differential Toxicity |
URI | http://dx.doi.org/10.1021/jp506509c https://www.ncbi.nlm.nih.gov/pubmed/25322200 https://search.proquest.com/docview/1660400629 https://search.proquest.com/docview/1762066712 |
Volume | 119 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwhV1LTwIxEG4QD3rx_cAHqY_r4tLd7e4eFSTEqBcg4Ub6TFCyS2BJjH_Cv-y07BKJgtdNO213pp1v0uk3CN2Cz3Mp96ij6ix2_JBKhykftjshKgpEXPeZCRRfXmm75z_1g34J3ay4wSf1u7dxYGnexAbaJCGE3Qb_NDqLqCogtpwj-CETB7m0oA_62dW4HjFddj0r8KT1K61d1Cxe58zTSd5rs4zXxOdvssZ1U95DOzmuxPdzQ9hHJZUcoK1GUc7tEH09DNNxrhTcWKZpxqmGT-lITRjuph_DBLNE4sepUejQJENjMJchbsO57TwbSl6FbTJBmtnGHctBO5so220xJjblO3GW4mZehAUOk5GVLwD6H6Fe67HbaDt5NQaHgVfPHIB6gmkWCYg4Y99jPFaaEhm4kirP87R2heKSR2EchQRApJaaMxoy4QotiCe9Y1RO0kSdmnfiOo6YFCFXEUiKGeWGBAhkS1OpIqqgKqhrkO-m6cBelBMIVIr_WkHXhSYH4zkrx1-NrgodD2Dd5iKEJSqdgTxKzdlFSbymDXgJkwBcJxV0MjeQxVCwPIBVrnv23zzP0TYALJMd6RBygcqgDnUJICbjVWvE3z_i7YI |
link.rule.ids | 314,780,784,2765,27076,27924,27925,56738,56788 |
linkProvider | American Chemical Society |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1LT9tAEF619JBegJZXoNAFcTU4a3ttH2kApRBySSJxs_YpBSI7wo6E-BP8ZWY2dgoVfVyt9exjZne-0c5-Q8gx-Dyfy4B7piNSL4y59oQJYbszZpJIpZ1QYKB4M-C9cXh1G93WNDn4FgYGUYKk0l3i_2IX6JzezSLH9qY-kk8RlqpEGNQdLoOriLmqjuCOMBzyecMi9PpX9ECqfOuB_gArnXu5XFvUKXIDc1kl9yfzSp6op984G_9v5OtktUaZ9GxhFl_IB5N_Ja1uU9xtgzz_mBSzWkW0-5a0mRYWPhVT8yDoqHic5FTkml6UqN4JpkZTMJ4J7cEp7vWRoNdQl1pQVK7x0DHSzh-M-23ZJ8VinrQq6HldkgWOlqmTryAQ2CTjy4tRt-fVtRk8AT6-8gD4KWFFoiD-TMNAyNRYznTka26CILDWV0ZqmcRpEjOAlFZbKXgslK-sYoEOtshKXuRmB1-N2zQRWsXSJCApFVwiJRDI1li3ImmTA1jWrN5bZeauzRmELc26tslRo9BstuDoeK_RYaPqDOaN1yIiN8Uc5HGOJxln6V_agM_AdOAOa5PthZ0su4LpAcjy_d1_jfM7afVGN_2s_3NwvUc-A_TCvEmPsW9kBVRj9gHeVPLA2fULOfn17w |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1ZT-MwELY4JOCF--iysGbFayB1Eid5hEJVlmslQOIt8ikVUFKRVEL8Cf7yzrhJBSuu18gZjz3jOeTxN4Tsgs_zuQy4Z9oi9cKYa0-YEI47YyaJVNoOBSaK5xe8dxP-uY1u60QR38IAEyVQKt0lPp7qgbY1wkB7_24QOcQ3NUmmI7CyWMJ10LkaJ1gRc50dwSVhSuTzBkno9a_ohVT51gt9EFo6F9NdIJdj5lxlyf3esJJ76vk_3Mbvc79I5utokx6M1GOJTJh8mcx2miZvK-TlsF8MalHRzlvwZlpY-FQ8mEdBr4unfk5FrulxiWLuY4k0BSXq0x5Yc-8MgXoNdSUGReUGXzlk2uGjcb-N56TY1JNWBT2qW7OAiXlw9BUkBKvkpnt83el5dY8GT4CvrzwIAJWwIlGQh6ZhIGRqLGc68jU3QRBY6ysjtUziNIkZhJZWWyl4LJSvrGKBDtbIVF7kZgNfj9s0EVrF0iRAKRVcIjQQ0NbYvyJpkW3Y2qw-Y2Xmrs8ZpC_NvrbI70ao2WCE1fHeoJ1G3BmsG69HRG6KIdDjHC0aZ-knY8B3YFlwm7XI-khXxlPB8iDY8v0fX_H5i8z8PepmZycXp5tkDiIwLJ_0GPtJpkAyZguinEpuO9X-ByyK-HI |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Biophysical+Characteristics+of+Cholera+Toxin+and+Escherichia+coli+Heat-Labile+Enterotoxin+Structure+and+Chemistry+Lead+to+Differential+Toxicity&rft.jtitle=The+journal+of+physical+chemistry.+B&rft.au=Craft%2C+John+W&rft.au=Shen%2C+Tsai-wei&rft.au=Brier%2C+Lindsey+M&rft.au=Briggs%2C+James+M&rft.date=2015-01-22&rft.issn=1520-6106&rft.eissn=1520-5207&rft.volume=119&rft.issue=3&rft.spage=1048&rft.epage=1061&rft_id=info:doi/10.1021%2Fjp506509c&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1520-6106&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1520-6106&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1520-6106&client=summon |