139 related articles for article (PubMed ID: 2481497)
1. Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor.
Manning MC; Woody RW
Biochemistry; 1989 Oct; 28(21):8609-13. PubMed ID: 2481497
[TBL] [Abstract][Full Text] [Related]
2. Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitor.
Sreerama N; Manning MC; Powers ME; Zhang JX; Goldenberg DP; Woody RW
Biochemistry; 1999 Aug; 38(33):10814-22. PubMed ID: 10451378
[TBL] [Abstract][Full Text] [Related]
3. Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI). I. 1H NMR studies.
Wagner G; DeMarco A; Wüthrich K
Biophys Struct Mech; 1976 Aug; 2(2):139-58. PubMed ID: 9165
[TBL] [Abstract][Full Text] [Related]
4. Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding.
Kemmink J; Creighton TE
J Mol Biol; 1993 Dec; 234(3):861-78. PubMed ID: 7504737
[TBL] [Abstract][Full Text] [Related]
5. DichroCalc: Improvements in Computing Protein Circular Dichroism Spectroscopy in the Near-Ultraviolet.
Jasim SB; Li Z; Guest EE; Hirst JD
J Mol Biol; 2018 Jul; 430(15):2196-2202. PubMed ID: 29258819
[TBL] [Abstract][Full Text] [Related]
6. Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance.
Wagner G; Brühwiler D; Wüthrich K
J Mol Biol; 1987 Jul; 196(1):227-31. PubMed ID: 2443716
[TBL] [Abstract][Full Text] [Related]
7. The stabilizing effects of hydrophobic cores on peptide folding of bovine-pancreatic-trypsin-inhibitor folding-intermediate model.
Kwon DY
Eur J Biochem; 1994 Jul; 223(2):631-6. PubMed ID: 7519984
[TBL] [Abstract][Full Text] [Related]
8. Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains.
Vuilleumier S; Sancho J; Loewenthal R; Fersht AR
Biochemistry; 1993 Oct; 32(39):10303-13. PubMed ID: 8399173
[TBL] [Abstract][Full Text] [Related]
9. First-principles calculations of protein circular dichroism in the near ultraviolet.
Rogers DM; Hirst JD
Biochemistry; 2004 Aug; 43(34):11092-102. PubMed ID: 15323568
[TBL] [Abstract][Full Text] [Related]
10. Direct evidence for alteration of unfolding profile of a helical peptide by far-ultraviolet circular dichroism aromatic side-chain contribution.
Banerjee R; Basu G
FEBS Lett; 2002 Jul; 523(1-3):152-6. PubMed ID: 12123823
[TBL] [Abstract][Full Text] [Related]
11. Vacuum-Ultraviolet Circular Dichroism Spectra of Escherichia coli Dihydrofolate Reductase and Its Mutants: Contributions of Phenylalanine and Tyrosine Side Chains and Exciton Coupling of Two Tryptophan Side Chains.
Ohmae E; Tanaka S; Miyashita Y; Katayanagi K; Matsuo K
J Phys Chem B; 2015 Oct; 119(41):13002-8. PubMed ID: 26407224
[TBL] [Abstract][Full Text] [Related]
12. Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor.
Kosen PA; Creighton TE; Blout ER
Biochemistry; 1981 Sep; 20(20):5744-54. PubMed ID: 7295701
[TBL] [Abstract][Full Text] [Related]
13. Ultraviolet difference spectroscopy of intermediates trapped in unfolding and refolding of bovine pancreatic trypsin inhibitor.
Kosen PA; Creighton TE; Blout ER
Biochemistry; 1980 Oct; 19(21):4936-44. PubMed ID: 7426636
[TBL] [Abstract][Full Text] [Related]
14. Correcting the circular dichroism spectra of peptides for contributions of absorbing side chains.
Krittanai C; Johnson WC
Anal Biochem; 1997 Nov; 253(1):57-64. PubMed ID: 9356142
[TBL] [Abstract][Full Text] [Related]
15. Structure of single-disulfide variants of bovine pancreatic trypsin inhibitor (BPTI) as probed by their binding to bovine beta-trypsin.
Krokoszynska I; Dadlez M; Otlewski J
J Mol Biol; 1998 Jan; 275(3):503-13. PubMed ID: 9466927
[TBL] [Abstract][Full Text] [Related]
16. Circular dichroism spectroscopy of the intermediates that precede the rate-limiting step of the refolding pathway of bovine pancreatic trypsin inhibitor. Relationship of conformation and the refolding pathway.
Kosen PA; Creighton TE; Blout ER
Biochemistry; 1983 May; 22(10):2433-40. PubMed ID: 6860640
[TBL] [Abstract][Full Text] [Related]
17. Characterization of intermolecular structure of β(2)-microglobulin core fragments in amyloid fibrils by vacuum-ultraviolet circular dichroism spectroscopy and circular dichroism theory.
Matsuo K; Hiramatsu H; Gekko K; Namatame H; Taniguchi M; Woody RW
J Phys Chem B; 2014 Mar; 118(11):2785-95. PubMed ID: 24512563
[TBL] [Abstract][Full Text] [Related]
18. Native-like conformations are sampled by partially folded and disordered variants of bovine pancreatic trypsin inhibitor.
Tulla-Puche J; Getun IV; Woodward C; Barany G
Biochemistry; 2004 Feb; 43(6):1591-8. PubMed ID: 14769035
[TBL] [Abstract][Full Text] [Related]
19. Folding of a peptide corresponding to the alpha-helix in bovine pancreatic trypsin inhibitor.
Goodman EM; Kim PS
Biochemistry; 1989 May; 28(10):4343-7. PubMed ID: 2765489
[TBL] [Abstract][Full Text] [Related]
20. Determination of the contributions of individual aromatic residues to the CD spectrum of IL-1 beta using site directed mutagenesis.
Craig S; Pain RH; Schmeissner U; Virden R; Wingfield PT
Int J Pept Protein Res; 1989 Apr; 33(4):256-62. PubMed ID: 2787788
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
