Protein folding: Pulling back the frontiers

Current Biology

Volumn 10, Issue 18, 2000, Pages R662-R664

  Smith, D Alastair ^a   Radford, Sheena E ^a  

^a UNIVERSITY OF LEEDS   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; MEMBRANE PROTEIN; MUSCLE PROTEIN; PROTEIN KINASE;

ARTICLE; ATOMIC FORCE MICROSCOPY; CHEMISTRY; ELASTICITY; MECHANICAL STRESS; METABOLISM; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE;

ELASTICITY; MEMBRANE PROTEINS; MICROSCOPY, ATOMIC FORCE; MUSCLE PROTEINS; PROTEIN FOLDING; PROTEIN KINASES; PROTEIN STRUCTURE, TERTIARY; STRESS, MECHANICAL; SUPPORT, NON-U.S. GOV'T;

EID: 0034699342     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00681-3     Document Type: Review

References (12)

1. Structure and distribution of modules in extracellular proteins
2. The study of protein mechanics with the atomic force microscope
3. Folding-unfolding transitions in single titin molecules characterised with laser tweezers
4. Sensitive force technique to probe molecular adhesion and structural linkages at biological interfaces
5. Mechanical and chemical unfolding of a single protein: A comparison
6. The mechanical stability of immunoglobulin and fibronectin III domains in the muscle protein titin measured by atomic force microscopy
7. Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch
8. Unfolding pathways of individual bacteriorhodopsins
9. Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
10. The molecular elasticity of the extracellular matrix protein tenascin
11. Atomic force microscopy reveals the mechanical design of a modular protein
12. The elastic I band region of titin is assembled in a 'modular' fashion by weakly interacting Ig-like domains