Measurement of the Length of the .ALPHA. Helical Section of a Peptide Directly Using Atomic Force Microscopy.
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- TAKEDA Seiji
- Tissue Engineering Research Center (TERC), National Institute of Advanced Industrial Science and Technology (AIST)
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- PTAK Arkadiusz
- Tissue Engineering Research Center (TERC), National Institute of Advanced Industrial Science and Technology (AIST)
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- NAKAMURA Chikashi
- Tissue Engineering Research Center (TERC), National Institute of Advanced Industrial Science and Technology (AIST)
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- MIYAKE Jun
- Tissue Engineering Research Center (TERC), National Institute of Advanced Industrial Science and Technology (AIST)
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- KAGESHIMA Masami
- Joint Research Center for Atom Technology (JRCAT)
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- JARVIS Suzanne P.
- Joint Research Center for Atom Technology (JRCAT)
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- TOKUMOTO Hiroshi
- Joint Research Center for Atom Technology (JRCAT)
Bibliographic Information
- Other Title
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- Measurement of the Length of the α Helical Section of a Peptide Directly Using Atomic Force Microscopy
- Measurement of the Length of the アルファ Helical Section of a Peptide Directly Using Atomic Force Microscopy
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Abstract
Using atomic force microscopy (AFM), the length of the α-helix structure of poly-L-lysine was investigated by stretching the peptide directly, one molecule at a time. In the absence of urea, many rupturing points that seemed to be due to the breaking of some hydrogen bonds were observed in force-extension curves, while these points were never observed in the presence of 8 M urea. In the presence of 0.4 or 1.6 M urea, both force-extension curve types were observed. Total peptide elongation for each condition was calculated from force-extension curves reflecting the α-helix rupturing process. The experimental value of total elongation divided by the theoretical value of total α-helix elongation yields the α-helix content. This value was compatible with circular dichroism (CD) measurement results. This suggests that peptide conformation and content of the α-helix on a single molecule scale can be investigated by direct mechanical measurement using atomic force microscopy.
Journal
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- Chemical and Pharmaceutical Bulletin
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Chemical and Pharmaceutical Bulletin 49 (12), 1512-1516, 2001
The Pharmaceutical Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679138356736
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- NII Article ID
- 110003615828
- 30023110307
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- NII Book ID
- AA00602100
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- COI
- 1:CAS:528:DC%2BD3MXosl2rsL8%3D
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- ISSN
- 13475223
- 00092363
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- NDL BIB ID
- 5995152
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- PubMed
- 11767067
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- Abstract License Flag
- Disallowed