Basic fibroblast growth factor is a β-rich protein
| ISSN: |
1573-4943
|
|---|---|
| Keywords: |
Basic fibroblast growth factor ; circular dichroism ; trifluoroethanol ; sodium dodecyl sulfate
|
| Source: |
Springer Online Journal Archives 1860-2000
|
| Topics: |
Chemistry and Pharmacology
|
| Notes: |
Abstract The conformation of the 153-residue form of human basic fibroblast growth factor (bFGF) was studied with circular dichroism (CD) and sequence prediction methods. The far-UV CD spectrum with a minimum at 202 nm resembled that of an unordered polypeptide/protein or a protein rich in distorted antiparallel β-sheets. Analysis of the CD spectrum by the least-squares method of Changet al. (1978) and the CONTIN program of Provencher and Glöckner (1981) suggested that about one half of the molecule consisted of β-sheet and there was no α-helix. These estimates agreed with the prediction by the sequence method of Garnieret al. (1978) using decision constants based on CD results. bFGF had an unusual CD band at 187 nm, which disappeared upon ionization of Tyr side chains atpH 11.7. It also had another unusual property of irreversibly converting the CD spectrum to a helix-like one with a double minimum at 205 and 215 and a maximum at 189 nm upon heating the solution to above 55°C. The helicity was also enhanced in trifluoroethanol and in sodium dodecyl sulfate. The mutant bFGF in which cysteines 76 and 94 were replaced by serine residues had essentially the same properties as the wild-type.
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798296777311387648 |
|---|---|
| autor | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi |
| autorsonst | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi |
| book_url | http://dx.doi.org/10.1007/BF01025257 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLM197804578 |
| issn | 1573-4943 |
| journal_name | The protein journal |
| materialart | 1 |
| notes | Abstract The conformation of the 153-residue form of human basic fibroblast growth factor (bFGF) was studied with circular dichroism (CD) and sequence prediction methods. The far-UV CD spectrum with a minimum at 202 nm resembled that of an unordered polypeptide/protein or a protein rich in distorted antiparallel β-sheets. Analysis of the CD spectrum by the least-squares method of Changet al. (1978) and the CONTIN program of Provencher and Glöckner (1981) suggested that about one half of the molecule consisted of β-sheet and there was no α-helix. These estimates agreed with the prediction by the sequence method of Garnieret al. (1978) using decision constants based on CD results. bFGF had an unusual CD band at 187 nm, which disappeared upon ionization of Tyr side chains atpH 11.7. It also had another unusual property of irreversibly converting the CD spectrum to a helix-like one with a double minimum at 205 and 215 and a maximum at 189 nm upon heating the solution to above 55°C. The helicity was also enhanced in trifluoroethanol and in sodium dodecyl sulfate. The mutant bFGF in which cysteines 76 and 94 were replaced by serine residues had essentially the same properties as the wild-type. |
| package_name | Springer |
| publikationsjahr_anzeige | 1991 |
| publikationsjahr_facette | 1991 |
| publikationsjahr_intervall | 8009:1990-1994 |
| publikationsjahr_sort | 1991 |
| publisher | Springer |
| reference | 10 (1991), S. 427-436 |
| schlagwort | Basic fibroblast growth factor circular dichroism trifluoroethanol sodium dodecyl sulfate |
| search_space | articles |
| shingle_author_1 | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi |
| shingle_author_2 | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi |
| shingle_author_3 | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi |
| shingle_author_4 | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi |
| shingle_catch_all_1 | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi Basic fibroblast growth factor is a β-rich protein Basic fibroblast growth factor circular dichroism trifluoroethanol sodium dodecyl sulfate Basic fibroblast growth factor circular dichroism trifluoroethanol sodium dodecyl sulfate Abstract The conformation of the 153-residue form of human basic fibroblast growth factor (bFGF) was studied with circular dichroism (CD) and sequence prediction methods. The far-UV CD spectrum with a minimum at 202 nm resembled that of an unordered polypeptide/protein or a protein rich in distorted antiparallel β-sheets. Analysis of the CD spectrum by the least-squares method of Changet al. (1978) and the CONTIN program of Provencher and Glöckner (1981) suggested that about one half of the molecule consisted of β-sheet and there was no α-helix. These estimates agreed with the prediction by the sequence method of Garnieret al. (1978) using decision constants based on CD results. bFGF had an unusual CD band at 187 nm, which disappeared upon ionization of Tyr side chains atpH 11.7. It also had another unusual property of irreversibly converting the CD spectrum to a helix-like one with a double minimum at 205 and 215 and a maximum at 189 nm upon heating the solution to above 55°C. The helicity was also enhanced in trifluoroethanol and in sodium dodecyl sulfate. The mutant bFGF in which cysteines 76 and 94 were replaced by serine residues had essentially the same properties as the wild-type. 1573-4943 15734943 Springer |
| shingle_catch_all_2 | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi Basic fibroblast growth factor is a β-rich protein Basic fibroblast growth factor circular dichroism trifluoroethanol sodium dodecyl sulfate Basic fibroblast growth factor circular dichroism trifluoroethanol sodium dodecyl sulfate Abstract The conformation of the 153-residue form of human basic fibroblast growth factor (bFGF) was studied with circular dichroism (CD) and sequence prediction methods. The far-UV CD spectrum with a minimum at 202 nm resembled that of an unordered polypeptide/protein or a protein rich in distorted antiparallel β-sheets. Analysis of the CD spectrum by the least-squares method of Changet al. (1978) and the CONTIN program of Provencher and Glöckner (1981) suggested that about one half of the molecule consisted of β-sheet and there was no α-helix. These estimates agreed with the prediction by the sequence method of Garnieret al. (1978) using decision constants based on CD results. bFGF had an unusual CD band at 187 nm, which disappeared upon ionization of Tyr side chains atpH 11.7. It also had another unusual property of irreversibly converting the CD spectrum to a helix-like one with a double minimum at 205 and 215 and a maximum at 189 nm upon heating the solution to above 55°C. The helicity was also enhanced in trifluoroethanol and in sodium dodecyl sulfate. The mutant bFGF in which cysteines 76 and 94 were replaced by serine residues had essentially the same properties as the wild-type. 1573-4943 15734943 Springer |
| shingle_catch_all_3 | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi Basic fibroblast growth factor is a β-rich protein Basic fibroblast growth factor circular dichroism trifluoroethanol sodium dodecyl sulfate Basic fibroblast growth factor circular dichroism trifluoroethanol sodium dodecyl sulfate Abstract The conformation of the 153-residue form of human basic fibroblast growth factor (bFGF) was studied with circular dichroism (CD) and sequence prediction methods. The far-UV CD spectrum with a minimum at 202 nm resembled that of an unordered polypeptide/protein or a protein rich in distorted antiparallel β-sheets. Analysis of the CD spectrum by the least-squares method of Changet al. (1978) and the CONTIN program of Provencher and Glöckner (1981) suggested that about one half of the molecule consisted of β-sheet and there was no α-helix. These estimates agreed with the prediction by the sequence method of Garnieret al. (1978) using decision constants based on CD results. bFGF had an unusual CD band at 187 nm, which disappeared upon ionization of Tyr side chains atpH 11.7. It also had another unusual property of irreversibly converting the CD spectrum to a helix-like one with a double minimum at 205 and 215 and a maximum at 189 nm upon heating the solution to above 55°C. The helicity was also enhanced in trifluoroethanol and in sodium dodecyl sulfate. The mutant bFGF in which cysteines 76 and 94 were replaced by serine residues had essentially the same properties as the wild-type. 1573-4943 15734943 Springer |
| shingle_catch_all_4 | Wu, Chuen-Shang C. Thompson, Stewart A. Yang, Jen Tsi Basic fibroblast growth factor is a β-rich protein Basic fibroblast growth factor circular dichroism trifluoroethanol sodium dodecyl sulfate Basic fibroblast growth factor circular dichroism trifluoroethanol sodium dodecyl sulfate Abstract The conformation of the 153-residue form of human basic fibroblast growth factor (bFGF) was studied with circular dichroism (CD) and sequence prediction methods. The far-UV CD spectrum with a minimum at 202 nm resembled that of an unordered polypeptide/protein or a protein rich in distorted antiparallel β-sheets. Analysis of the CD spectrum by the least-squares method of Changet al. (1978) and the CONTIN program of Provencher and Glöckner (1981) suggested that about one half of the molecule consisted of β-sheet and there was no α-helix. These estimates agreed with the prediction by the sequence method of Garnieret al. (1978) using decision constants based on CD results. bFGF had an unusual CD band at 187 nm, which disappeared upon ionization of Tyr side chains atpH 11.7. It also had another unusual property of irreversibly converting the CD spectrum to a helix-like one with a double minimum at 205 and 215 and a maximum at 189 nm upon heating the solution to above 55°C. The helicity was also enhanced in trifluoroethanol and in sodium dodecyl sulfate. The mutant bFGF in which cysteines 76 and 94 were replaced by serine residues had essentially the same properties as the wild-type. 1573-4943 15734943 Springer |
| shingle_title_1 | Basic fibroblast growth factor is a β-rich protein |
| shingle_title_2 | Basic fibroblast growth factor is a β-rich protein |
| shingle_title_3 | Basic fibroblast growth factor is a β-rich protein |
| shingle_title_4 | Basic fibroblast growth factor is a β-rich protein |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Springer Online Journal Archives 1860-2000 |
| timestamp | 2024-05-06T09:57:29.589Z |
| titel | Basic fibroblast growth factor is a β-rich protein |
| titel_suche | Basic fibroblast growth factor is a β-rich protein |
| topic | V |
| uid | nat_lic_papers_NLM197804578 |