Secondary structure in ribonuclease. II. Relations between folding kinetics and secondary structure elements
- PMID: 6286980
- DOI: 10.1016/0022-2836(82)90239-x
Secondary structure in ribonuclease. II. Relations between folding kinetics and secondary structure elements
Similar articles
-
Secondary structure in ribonuclease. I. Equilibrium folding transitions seen by amide circular dichroism.J Mol Biol. 1982 May 15;157(2):331-55. doi: 10.1016/0022-2836(82)90238-8. J Mol Biol. 1982. PMID: 6286979 No abstract available.
-
Local secondary structure in ribonuclease A denatured by guanidine . HCl near 1 degree C.J Mol Biol. 1982 Nov 25;162(1):173-86. doi: 10.1016/0022-2836(82)90167-x. J Mol Biol. 1982. PMID: 7154094 No abstract available.
-
Fast- and slow-refolding forms of unfolded ribonuclease A differ in tyrosine fluorescence.Biochemistry. 1982 Mar 30;21(7):1499-505. doi: 10.1021/bi00536a006. Biochemistry. 1982. PMID: 6282306 No abstract available.
-
Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding.Annu Rev Biochem. 1982;51:459-89. doi: 10.1146/annurev.bi.51.070182.002331. Annu Rev Biochem. 1982. PMID: 6287919 Review. No abstract available.
-
Folding of protein fragments.Adv Protein Chem. 1981;34:61-92. doi: 10.1016/s0065-3233(08)60518-5. Adv Protein Chem. 1981. PMID: 6266231 Review. No abstract available.
Cited by
-
Kinetic circular dichroism shows that the S-peptide alpha-helix of ribonuclease S unfolds fast and refolds slowly.Proc Natl Acad Sci U S A. 1984 Dec;81(24):7674-8. doi: 10.1073/pnas.81.24.7674. Proc Natl Acad Sci U S A. 1984. PMID: 6595655 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources