Thermally Denatured Ribonuclease A Retains Secondary Structure As Shown by FTIR
Fourier transform-infrared (FTIR) spectroscopy has been used to test for the presence of nonrandom structure in thermally denatured ribonuclease A (RNase A) at pH* 2.0 (uncorrected pH measured in D2O). The amide I spectral region of the native and thermally denatured protein was compared. A substant...
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| Veröffentlicht in: | Biochemistry (Easton) 1994-02, Vol.33 (6), p.1351-1355 |
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| creator | Seshadri, Sangita Oberg, Keith A Fink, Anthony L |
| description | Fourier transform-infrared (FTIR) spectroscopy has been used to test for the presence of nonrandom structure in thermally denatured ribonuclease A (RNase A) at pH* 2.0 (uncorrected pH measured in D2O). The amide I spectral region of the native and thermally denatured protein was compared. A substantial decrease in the amount of beta-sheet and alpha-helix and a corresponding increase in the amount of turn and unordered structure was observed on thermal denaturation. The results indicate that thermally denatured RNase A contains significant amounts of secondary structure (11% helix and 17% beta-sheet), consistent with previous results reported for circular dichroism, and with a relatively compact structure, as revealed by dynamic light scattering. These results are in contrast to those of amide protection experiments reported recently [Robertson, A.D., & Baldwin, R.L. (1991) Biochemistry 30, 9907-9914] which indicated no stable hydrogen-bonded structure under these experimental conditions. Possible explanations for this apparent discrepancy are given. |
| doi_str_mv | 10.1021/bi00172a010 |
| format | Article |
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The amide I spectral region of the native and thermally denatured protein was compared. A substantial decrease in the amount of beta-sheet and alpha-helix and a corresponding increase in the amount of turn and unordered structure was observed on thermal denaturation. The results indicate that thermally denatured RNase A contains significant amounts of secondary structure (11% helix and 17% beta-sheet), consistent with previous results reported for circular dichroism, and with a relatively compact structure, as revealed by dynamic light scattering. These results are in contrast to those of amide protection experiments reported recently [Robertson, A.D., & Baldwin, R.L. (1991) Biochemistry 30, 9907-9914] which indicated no stable hydrogen-bonded structure under these experimental conditions. Possible explanations for this apparent discrepancy are given.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00172a010</identifier><identifier>PMID: 8312253</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cattle ; Circular Dichroism ; Conformational dynamics in molecular biology ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. 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The amide I spectral region of the native and thermally denatured protein was compared. A substantial decrease in the amount of beta-sheet and alpha-helix and a corresponding increase in the amount of turn and unordered structure was observed on thermal denaturation. The results indicate that thermally denatured RNase A contains significant amounts of secondary structure (11% helix and 17% beta-sheet), consistent with previous results reported for circular dichroism, and with a relatively compact structure, as revealed by dynamic light scattering. These results are in contrast to those of amide protection experiments reported recently [Robertson, A.D., & Baldwin, R.L. (1991) Biochemistry 30, 9907-9914] which indicated no stable hydrogen-bonded structure under these experimental conditions. Possible explanations for this apparent discrepancy are given.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Circular Dichroism</subject><subject>Conformational dynamics in molecular biology</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hot Temperature</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydrolases</subject><subject>Molecular biophysics</subject><subject>Protein Denaturation</subject><subject>Protein Structure, Secondary</subject><subject>Ribonuclease, Pancreatic - chemistry</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1vEzEQBmALgUpaOHFG8gHRA1oYf6-PUUrTikpFSeBqeb2z6pbNbmvvCvLvcUkUcUDi5I95NJp5CXnD4CMDzj5VLQAz3AODZ2TGFIdCWquekxkA6IJbDS_JaUr3-SnByBNyUgrGuRIzcru5w7j1XbejF9j7cYpY01VbDf0UOvQJ6ZyucPRtn-gaw9DXPu7oeoxTeLJ0nr_vhp89rXb0cnO9ekVeNL5L-PpwnpFvl583i6vi5nZ5vZjfFF4yORYIUHJrQyW81bIJvkRAa6taGQ9Bm6YsfbAcTKNqZEGhzhdZ6bqqgtIGxBl5v-_7EIfHCdPotm0K2HW-x2FKzmihmJLiv5BpK7lVKsMPexjikFLExj3Edpu3dQzcU87ur5yzfntoO1VbrI_2EGyuvzvUfQq-a6LvQ5uOTFit1Z81ij1r04i_jmUffzhthFFu83Xtvi_F8svV4sItsz_fex-Sux-m2OeQ_zngby4sn4Q</recordid><startdate>19940201</startdate><enddate>19940201</enddate><creator>Seshadri, Sangita</creator><creator>Oberg, Keith A</creator><creator>Fink, Anthony L</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19940201</creationdate><title>Thermally Denatured Ribonuclease A Retains Secondary Structure As Shown by FTIR</title><author>Seshadri, Sangita ; Oberg, Keith A ; Fink, Anthony L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a414t-e008299cb3a964fca8e0e99bd57a0c67f88ac9207f5de1c5e6f5d4b6dbbc56703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Circular Dichroism</topic><topic>Conformational dynamics in molecular biology</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hot Temperature</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydrolases</topic><topic>Molecular biophysics</topic><topic>Protein Denaturation</topic><topic>Protein Structure, Secondary</topic><topic>Ribonuclease, Pancreatic - chemistry</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Seshadri, Sangita</creatorcontrib><creatorcontrib>Oberg, Keith A</creatorcontrib><creatorcontrib>Fink, Anthony L</creatorcontrib><collection>Istex</collection><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>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Seshadri, Sangita</au><au>Oberg, Keith A</au><au>Fink, Anthony L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thermally Denatured Ribonuclease A Retains Secondary Structure As Shown by FTIR</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1994-02-01</date><risdate>1994</risdate><volume>33</volume><issue>6</issue><spage>1351</spage><epage>1355</epage><pages>1351-1355</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Fourier transform-infrared (FTIR) spectroscopy has been used to test for the presence of nonrandom structure in thermally denatured ribonuclease A (RNase A) at pH* 2.0 (uncorrected pH measured in D2O). The amide I spectral region of the native and thermally denatured protein was compared. A substantial decrease in the amount of beta-sheet and alpha-helix and a corresponding increase in the amount of turn and unordered structure was observed on thermal denaturation. The results indicate that thermally denatured RNase A contains significant amounts of secondary structure (11% helix and 17% beta-sheet), consistent with previous results reported for circular dichroism, and with a relatively compact structure, as revealed by dynamic light scattering. These results are in contrast to those of amide protection experiments reported recently [Robertson, A.D., & Baldwin, R.L. (1991) Biochemistry 30, 9907-9914] which indicated no stable hydrogen-bonded structure under these experimental conditions. Possible explanations for this apparent discrepancy are given.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>8312253</pmid><doi>10.1021/bi00172a010</doi><tpages>5</tpages></addata></record> |
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| language | eng |
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| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Circular Dichroism Conformational dynamics in molecular biology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Hot Temperature Hydrogen-Ion Concentration Hydrolases Molecular biophysics Protein Denaturation Protein Structure, Secondary Ribonuclease, Pancreatic - chemistry Spectroscopy, Fourier Transform Infrared |
| title | Thermally Denatured Ribonuclease A Retains Secondary Structure As Shown by FTIR |
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