Atomic force microscopy study of the conformational change in immobilized calmodulin

© 2011 American Chemical Society

Bibliographische Detailangaben
Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 27(2011), 17 vom: 06. Sept., Seite 10793-9
1. Verfasser: Trajkovic, Sanja (VerfasserIn)
Weitere Verfasser: Zhang, Xiaoning, Daunert, Sylvia, Cai, Yuguang
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Calmodulin
LEADER 01000caa a22002652c 4500
001 NLM21002741X
003 DE-627
005 20250714190748.0
007 cr uuu---uuuuu
008 231224s2011 xx |||||o 00| ||eng c
024 7 |a 10.1021/la2016885  |2 doi 
028 5 2 |a pubmed25n1431.xml 
035 |a (DE-627)NLM21002741X 
035 |a (NLM)21766850 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Trajkovic, Sanja  |e verfasserin  |4 aut 
245 1 0 |a Atomic force microscopy study of the conformational change in immobilized calmodulin 
264 1 |c 2011 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 29.12.2011 
500 |a Date Revised 29.05.2025 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a © 2011 American Chemical Society 
520 |a Maintaining the biological functionality of immobilized proteins is the key to the success of numerous protein-based biomedical devices. To that end, we studied the conformational change in calmodulin (CaM) immobilized on chemical patterns. 1-Cysteine-mutated calmodulin was immobilized on a mercapto-terminated surface through cysteine-Hg-mercapto coupling. Utilizing atomic force microscopy (AFM), the average height of immobilized calmodulin was determined to be 1.87 ± 0.19 nm. After incubation in EGTA solution, the average height of the protein changed to 2.26 ± 0.21 nm, indicating the conformational change of CaM to Apo-CaM. Immobilized CaM also demonstrated a conformational change upon the reaction with known calmodulin antagonist chlorpromazine (CPZ). After incubation in CPZ solution, the average height of CPZ-bound CaM increased to 2.32 ± 0.20 nm, demonstrating that immobilized CaM has a similar response to that in bulk solution. These results show that the immobilization of calmodulin on a solid support does not interfere with the ability of the protein to bind calcium and calmodulin antagonists. Our results demonstrate the feasibility of employing AFM to probe and understand protein conformational changes 
650 4 |a Journal Article 
650 4 |a Research Support, N.I.H., Extramural 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
650 7 |a Calmodulin  |2 NLM 
700 1 |a Zhang, Xiaoning  |e verfasserin  |4 aut 
700 1 |a Daunert, Sylvia  |e verfasserin  |4 aut 
700 1 |a Cai, Yuguang  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Langmuir : the ACS journal of surfaces and colloids  |d 1985  |g 27(2011), 17 vom: 06. Sept., Seite 10793-9  |w (DE-627)NLM098181009  |x 1520-5827  |7 nnas 
773 1 8 |g volume:27  |g year:2011  |g number:17  |g day:06  |g month:09  |g pages:10793-9 
856 4 0 |u http://dx.doi.org/10.1021/la2016885  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_22 
912 |a GBV_ILN_350 
912 |a GBV_ILN_721 
951 |a AR 
952 |d 27  |j 2011  |e 17  |b 06  |c 09  |h 10793-9