Force as a probe of membrane protein structure and function.
Force measurement techniques are being used increasingly to explore the mechanical properties of proteins, as well as the structural origins of intermolecular forces. Developments in instrumentation and the increasing availability of engineered and purified membrane proteins have widely expanded the range of biological systems that can be addressed. Within the past year, force measurements have identified novel mechanisms of binding between cell-surface proteins, as well as the mechanical properties of integral membrane proteins and the intramolecular interactions that stabilize their structures.
Leckband
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Department of Chemical Engineering, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, IL 61801, USA. leckband@uiuc.edu
D015820:Cadherins / Q000378:metabolism; D007368:Interferometry; D008027:Light; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D013314:Stress, Mechanical; D013499:Surface Properties
D015820:Cadherins; D008565:Membrane Proteins