Insight into conformational changes of a single α-helix peptide molecule through stiffness measurements

Stiffness variations during the conformational change of a single α-helix polylysine peptide molecule were measured in a liquid environment using atomic force microscopy (AFM) with magnetic cantilever modulation. At the initial stage of the stretching process the stiffness decreased due to the break...

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Published inChemical physics letters Vol. 343; no. 1; pp. 77 - 82
Main Authors Kageshima, Masami, Lantz, Mark A., Jarvis, Suzanne P., Tokumoto, Hiroshi, Takeda, Seiji, Ptak, Arkadiusz, Nakamura, Chikashi, Miyake, Jun
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 27.07.2001
Elsevier Science
Subjects
Biological and medical sciences
Conformational dynamics in molecular biology
Dynamics and conformational changes
Fundamental and applied biological sciences. Psychology
Molecular biophysics
Helicoidal configuration
Atomic force microscopy
Lysine
Polypeptide
Mechanical properties
pH
Stiffness
Experimental study
Conformational changes
Stretching
Protein
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Abstract Stiffness variations during the conformational change of a single α-helix polylysine peptide molecule were measured in a liquid environment using atomic force microscopy (AFM) with magnetic cantilever modulation. At the initial stage of the stretching process the stiffness decreased due to the breaking of hydrogen bonds and then increased due to the stretching of the helix backbone. These changes were reversible on reversal of the stretching motion. Below p K, the stiffness did not show increase on reversal, indicating that the reforming of hydrogen bonds did not take place. Conformational changes in the molecule were examined via these changes in stiffness.
AbstractList Stiffness variations during the conformational change of a single α-helix polylysine peptide molecule were measured in a liquid environment using atomic force microscopy (AFM) with magnetic cantilever modulation. At the initial stage of the stretching process the stiffness decreased due to the breaking of hydrogen bonds and then increased due to the stretching of the helix backbone. These changes were reversible on reversal of the stretching motion. Below p K, the stiffness did not show increase on reversal, indicating that the reforming of hydrogen bonds did not take place. Conformational changes in the molecule were examined via these changes in stiffness.
Author Ptak, Arkadiusz
Miyake, Jun
Kageshima, Masami
Lantz, Mark A.
Takeda, Seiji
Tokumoto, Hiroshi
Jarvis, Suzanne P.
Nakamura, Chikashi
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  surname: Tokumoto
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  givenname: Jun
  surname: Miyake
  fullname: Miyake, Jun
  organization: National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8562, Japan
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Issue 1
Keywords Helicoidal configuration
Atomic force microscopy
Lysine
Polypeptide
Mechanical properties
pH
Stiffness
Experimental study
Conformational changes
Stretching
Protein
Language English
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Snippet Stiffness variations during the conformational change of a single α-helix polylysine peptide molecule were measured in a liquid environment using atomic force...
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SubjectTerms Biological and medical sciences
Conformational dynamics in molecular biology
Dynamics and conformational changes
Fundamental and applied biological sciences. Psychology
Molecular biophysics
Title Insight into conformational changes of a single α-helix peptide molecule through stiffness measurements
URI https://dx.doi.org/10.1016/S0009-2614(01)00678-9
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