Acid-Induced Folding of Proteins
The addition of HCl, at low ionic strength, to the native state of apomyoglobin, β-lactamase, and cytochrome c caused these proteins to adopt an essentially fully unfolded conformation in the vicinity of pH 2. However, contrary to expectation, the addition of further acid resulted in refolding to a...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1990-01, Vol.87 (2), p.573-577 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 87 |
| creator | Goto, Yuji Calciano, Linda J. Fink, Anthony L. |
| description | The addition of HCl, at low ionic strength, to the native state of apomyoglobin, β-lactamase, and cytochrome c caused these proteins to adopt an essentially fully unfolded conformation in the vicinity of pH 2. However, contrary to expectation, the addition of further acid resulted in refolding to a compact conformation with the properties of a molten globule. The major factor responsible for the refolding is believed to be the binding of the anion, which minimizes the intramolecular charge repulsion that initially brought about the unfolding. |
| doi_str_mv | 10.1073/pnas.87.2.573 |
| format | Article |
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However, contrary to expectation, the addition of further acid resulted in refolding to a compact conformation with the properties of a molten globule. The major factor responsible for the refolding is believed to be the binding of the anion, which minimizes the intramolecular charge repulsion that initially brought about the unfolding.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.87.2.573</identifier><identifier>PMID: 2153957</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Anions ; apomyoglobin ; Apoproteins - metabolism ; beta -lactamase ; Biochemistry ; Biological and medical sciences ; C.D ; Chlorides ; Circular Dichroism ; cytochrome c ; Cytochrome c Group - metabolism ; Cytochromes ; Fluorescence ; Fundamental and applied biological sciences. Psychology ; Globules ; Horses ; Hydrochloric Acid ; Hydrodynamics ; Hydrogen-Ion Concentration ; Kinetics ; Miscellaneous ; Myoglobin - metabolism ; Penicillinase - metabolism ; Protein Conformation ; Protein Denaturation ; Protein refolding ; Proteins ; Proteins - metabolism ; Spectrophotometry, Ultraviolet</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1990-01, Vol.87 (2), p.573-577</ispartof><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c578t-ec27f1d59d1862efc4327bfb49397f1f422b5b8a4d9e9109b09edec4836db6683</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/87/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2353552$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2353552$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,315,728,781,785,804,886,4025,27927,27928,27929,53795,53797,58021,58254</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6896715$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2153957$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goto, Yuji</creatorcontrib><creatorcontrib>Calciano, Linda J.</creatorcontrib><creatorcontrib>Fink, Anthony L.</creatorcontrib><title>Acid-Induced Folding of Proteins</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The addition of HCl, at low ionic strength, to the native state of apomyoglobin, β-lactamase, and cytochrome c caused these proteins to adopt an essentially fully unfolded conformation in the vicinity of pH 2. However, contrary to expectation, the addition of further acid resulted in refolding to a compact conformation with the properties of a molten globule. The major factor responsible for the refolding is believed to be the binding of the anion, which minimizes the intramolecular charge repulsion that initially brought about the unfolding.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Anions</subject><subject>apomyoglobin</subject><subject>Apoproteins - metabolism</subject><subject>beta -lactamase</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>C.D</subject><subject>Chlorides</subject><subject>Circular Dichroism</subject><subject>cytochrome c</subject><subject>Cytochrome c Group - metabolism</subject><subject>Cytochromes</subject><subject>Fluorescence</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Globules</subject><subject>Horses</subject><subject>Hydrochloric Acid</subject><subject>Hydrodynamics</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Miscellaneous</subject><subject>Myoglobin - metabolism</subject><subject>Penicillinase - metabolism</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>Protein refolding</subject><subject>Proteins</subject><subject>Proteins - metabolism</subject><subject>Spectrophotometry, Ultraviolet</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtPGzEURq2qCELaJbsiZVHYTer3Q-oGRQSQkGDRri2PH3TQZJzaM1X59zhiksAGVndxju_9_AFwguAcQUF-rDuT51LM8ZwJ8glMEFSo4lTBz2ACIRaVpJgegeOcHyGEikl4CA4xYkQxMQGzC9u46qZzg_Vutoyta7qHWQyz-xR733T5CzgIps3-6zin4Pfy8tfiurq9u7pZXNxWlgnZV95iEZBjyiHJsQ-WEizqUFNFVAGBYlyzWhrqlFclYg2Vd95SSbirOZdkCn6-7F0P9co767s-mVavU7My6UlH0-i3pGv-6If4TzNCSg1TcD4-T_Hv4HOvV022vm1N5-OQtVAcYg7lhyJiVFDIVBGrF9GmmHPyYZcFQb1pXm-a11JorEvzxT99_YGdPVZd-PeRm2xNG5LpbJN3GpeKi6JOwdmobbZv6faKDkPb9v5_X7xv73h7_Jj7mPZhCCOMYfIM-persg</recordid><startdate>19900101</startdate><enddate>19900101</enddate><creator>Goto, Yuji</creator><creator>Calciano, Linda J.</creator><creator>Fink, Anthony L.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19900101</creationdate><title>Acid-Induced Folding of Proteins</title><author>Goto, Yuji ; Calciano, Linda J. ; Fink, Anthony L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c578t-ec27f1d59d1862efc4327bfb49397f1f422b5b8a4d9e9109b09edec4836db6683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Anions</topic><topic>apomyoglobin</topic><topic>Apoproteins - metabolism</topic><topic>beta -lactamase</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>C.D</topic><topic>Chlorides</topic><topic>Circular Dichroism</topic><topic>cytochrome c</topic><topic>Cytochrome c Group - metabolism</topic><topic>Cytochromes</topic><topic>Fluorescence</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Globules</topic><topic>Horses</topic><topic>Hydrochloric Acid</topic><topic>Hydrodynamics</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Miscellaneous</topic><topic>Myoglobin - metabolism</topic><topic>Penicillinase - metabolism</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>Protein refolding</topic><topic>Proteins</topic><topic>Proteins - metabolism</topic><topic>Spectrophotometry, Ultraviolet</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goto, Yuji</creatorcontrib><creatorcontrib>Calciano, Linda J.</creatorcontrib><creatorcontrib>Fink, Anthony L.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goto, Yuji</au><au>Calciano, Linda J.</au><au>Fink, Anthony L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Acid-Induced Folding of Proteins</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1990-01-01</date><risdate>1990</risdate><volume>87</volume><issue>2</issue><spage>573</spage><epage>577</epage><pages>573-577</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>The addition of HCl, at low ionic strength, to the native state of apomyoglobin, β-lactamase, and cytochrome c caused these proteins to adopt an essentially fully unfolded conformation in the vicinity of pH 2. However, contrary to expectation, the addition of further acid resulted in refolding to a compact conformation with the properties of a molten globule. The major factor responsible for the refolding is believed to be the binding of the anion, which minimizes the intramolecular charge repulsion that initially brought about the unfolding.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2153957</pmid><doi>10.1073/pnas.87.2.573</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1990-01, Vol.87 (2), p.573-577 |
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| language | eng |
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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Analytical, structural and metabolic biochemistry Animals Anions apomyoglobin Apoproteins - metabolism beta -lactamase Biochemistry Biological and medical sciences C.D Chlorides Circular Dichroism cytochrome c Cytochrome c Group - metabolism Cytochromes Fluorescence Fundamental and applied biological sciences. Psychology Globules Horses Hydrochloric Acid Hydrodynamics Hydrogen-Ion Concentration Kinetics Miscellaneous Myoglobin - metabolism Penicillinase - metabolism Protein Conformation Protein Denaturation Protein refolding Proteins Proteins - metabolism Spectrophotometry, Ultraviolet |
| title | Acid-Induced Folding of Proteins |
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