Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 133

1.

Conservation of inter-residue interactions and prediction of folding rates of domain repeats.

Mary RD, Saravanan MK, Selvaraj S.

J Biomol Struct Dyn. 2015;33(3):534-51. doi: 10.1080/07391102.2014.894944. Epub 2014 Apr 7.

PMID:
24702623
2.
3.
4.

Underlying hydrophobic sequence periodicity of protein tertiary structure.

Silverman BD.

J Biomol Struct Dyn. 2005 Feb;22(4):411-23.

PMID:
15588105
6.

Relationship between protein folding kinetics and amino acid properties.

Huang JT, Xing DJ, Huang W.

Amino Acids. 2012 Aug;43(2):567-72. doi: 10.1007/s00726-011-1189-3. Epub 2011 Dec 13.

PMID:
22160260
7.

Structural determinants in protein folding: a single conserved hydrophobic residue determines folding of EGF domains.

Ng AS, Kini RM.

ACS Chem Biol. 2013 Jan 18;8(1):161-9. doi: 10.1021/cb300445a. Epub 2012 Oct 24.

PMID:
23094971
11.

Sequence and structural analysis of two designed proteins with 88% identity adopting different folds.

Saravanan KM, Balasubramanian H, Nallusamy S, Samuel S.

Protein Eng Des Sel. 2010 Dec;23(12):911-8. doi: 10.1093/protein/gzq070. Epub 2010 Oct 15.

PMID:
20952437
12.
13.
14.

The relationship between conservation, thermodynamic stability, and function in the SH3 domain hydrophobic core.

Di Nardo AA, Larson SM, Davidson AR.

J Mol Biol. 2003 Oct 24;333(3):641-55.

PMID:
14556750
15.

The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models.

Serrano L, Matouschek A, Fersht AR.

J Mol Biol. 1992 Apr 5;224(3):847-59.

PMID:
1569561
16.

Effects of turn stability and side-chain hydrophobicity on the folding of β-structures.

Shao Q, Wei H, Gao YQ.

J Mol Biol. 2010 Sep 24;402(3):595-609. doi: 10.1016/j.jmb.2010.08.037. Epub 2010 Sep 8.

PMID:
20804769
17.

The PAS fold. A redefinition of the PAS domain based upon structural prediction.

Hefti MH, Françoijs KJ, de Vries SC, Dixon R, Vervoort J.

Eur J Biochem. 2004 Mar;271(6):1198-208.

PMID:
15009198
18.
19.

The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.

Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE.

Curr Biol. 1997 Apr 1;7(4):239-45.

20.

Expansion of protein domain repeats.

Björklund AK, Ekman D, Elofsson A.

PLoS Comput Biol. 2006 Aug 25;2(8):e114. Epub 2006 Jul 14.

Supplemental Content

Support Center