Nucleation, rapid folding, and globular intrachain regions in proteins - PubMed (original) (raw)

Nucleation, rapid folding, and globular intrachain regions in proteins

D B Wetlaufer. Proc Natl Acad Sci U S A. 1973 Mar.

Abstract

Distinct structural regions have been found in several globular proteins composed of single polypeptide chains. The existence of such regions and the continuity of peptide chain within them, coupled with kinetic arguments, suggests that the early stages of three-dimensional structure formation (nucleation) occur independently in separate parts of these molecules. A nucleus can grow rapidly by adding peptide chain segments that are close to the nucleus in aminoacid sequence. Such a process would generate three-dimensional (native) protein structures that contain separate regions of continuous peptide chain. Possible means of testing this hypothesis are discussed.

PubMed Disclaimer

Similar articles

• Prediction of the amount of secondary structure in a globular protein from its aminoacid composition.
  Krigbaum WR, Knutton SP. Krigbaum WR, et al. Proc Natl Acad Sci U S A. 1973 Oct;70(10):2809-13. doi: 10.1073/pnas.70.10.2809. Proc Natl Acad Sci U S A. 1973. PMID: 4355367 Free PMC article.
• X-ray studies of crystalline proteins.
  Blake CC. Blake CC. Prog Biophys Mol Biol. 1972;25:85-130. doi: 10.1016/0079-6107(72)90017-x. Prog Biophys Mol Biol. 1972. PMID: 4575109 Review. No abstract available.
• Factors determining the formation of the tertiary structure of globular protein.
  Esipova NG, Tumanyan VG. Esipova NG, et al. Mol Biol. 1972 Nov-Dec;6(6):679-87. Mol Biol. 1972. PMID: 4667574 No abstract available.
• [Far interactions and their relation to secondary structure in globular proteins].
  Lim VI. Lim VI. Dokl Akad Nauk SSSR. 1972 Mar;203(2):480-2. Dokl Akad Nauk SSSR. 1972. PMID: 5062489 Russian. No abstract available.
• Transients and relaxation kinetics of enzyme reactions.
  Gutfreund H. Gutfreund H. Annu Rev Biochem. 1971;40:315-44. doi: 10.1146/annurev.bi.40.070171.001531. Annu Rev Biochem. 1971. PMID: 4330579 Review. No abstract available.

Cited by

• Mutational effects on the folding dynamics of a minimized hairpin.
  Scian M, Shu I, Olsen KA, Hassam K, Andersen NH. Scian M, et al. Biochemistry. 2013 Apr 16;52(15):2556-64. doi: 10.1021/bi400146c. Epub 2013 Apr 5. Biochemistry. 2013. PMID: 23521619 Free PMC article.
• Evolution of networks of protein domain organization.
  Aziz MF, Caetano-Anollés G. Aziz MF, et al. Sci Rep. 2021 Jun 8;11(1):12075. doi: 10.1038/s41598-021-90498-8. Sci Rep. 2021. PMID: 34103558 Free PMC article.
• Analysis of code relating sequences to conformation in globular prtoeins. Theory and application of expected information.
  Robson B. Robson B. Biochem J. 1974 Sep;141(3):853-67. doi: 10.1042/bj1410853. Biochem J. 1974. PMID: 4463965 Free PMC article.
• The search for local native-like nucleation centers in the unfolded state of beta -sheet proteins.
  Nikiforovich GV, Frieden C. Nikiforovich GV, et al. Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10388-93. doi: 10.1073/pnas.162362199. Epub 2002 Jul 24. Proc Natl Acad Sci U S A. 2002. PMID: 12140369 Free PMC article.
• Intrinsically disordered domains: Sequence ➔ disorder ➔ function relationships.
  Zhou J, Oldfield CJ, Yan W, Shen B, Dunker AK. Zhou J, et al. Protein Sci. 2019 Sep;28(9):1652-1663. doi: 10.1002/pro.3680. Epub 2019 Aug 9. Protein Sci. 2019. PMID: 31299122 Free PMC article.

References

1. 1. J Mol Biol. 1972 Jul 21;68(2):187-240 - PubMed
2. 1. J Biol Chem. 1965 Jan;240:299-303 - PubMed
3. 1. Cold Spring Harb Symp Quant Biol. 1972;36:125-40 - PubMed
4. 1. J Mol Biol. 1970 Jun 14;50(2):391-406 - PubMed
5. 1. Angew Chem Int Ed Engl. 1966 Feb;5(2):231-45 - PubMed

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Atypon
  • Europe PubMed Central
  • PubMed Central

• Other Literature Sources

  • The Lens - Patent Citations Database