Woes of proline: A cautionary kinetic tale

Protein Science

Volumn 15, Issue 3, 2006, Pages 393-394

  Pielak, Gary J ^a  

^a University of North Carolina at Chapel Hill   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROLINE;

CHEMICAL BINDING; CIS ISOMER; ISOMERIZATION; NOTE; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN VARIANT; THERMODYNAMICS; TRANS ISOMER; WILD TYPE;

CASPASES; KINETICS; MODELS, CHEMICAL; PROLINE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY;

EID: 33644526958     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.052051106     Document Type: Note

References (5)

1. Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science 181: 223-230.
2. Brandts, J.F., Halvorson, H.R., and Brennan, M. 1975. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14: 4953-4963.
3. Chen, Y.-R. and Clark, A.C. 2003. Equilibrium and kinetic folding of a α-helical Greek key protein domain: Caspase recruitment domain (CARD) of RICK. Biochemistry 42: 6310-6320.
4. _. 2006. Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK. Protein Sci. (this issue).
5. Schmid, F.X. 1983. Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates. Biochemistry 22: 4690-4696.