199 related articles for article (PubMed ID: 9787911)
1. Two-dimensional mid-IR and near-IR correlation spectra of ribonuclease A: using overtones and combination modes to monitor changes in secondary structure.
Schultz CP; Fabian H; Mantsch HH
Biospectroscopy; 1998; 4(5 Suppl):S19-29. PubMed ID: 9787911
[TBL] [Abstract][Full Text] [Related]
2. Secondary structure and temperature-induced unfolding and refolding of ribonuclease T1 in aqueous solution. A Fourier transform infrared spectroscopic study.
Fabian H; Schultz C; Naumann D; Landt O; Hahn U; Saenger W
J Mol Biol; 1993 Aug; 232(3):967-81. PubMed ID: 8355280
[TBL] [Abstract][Full Text] [Related]
3. Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution.
Dong A; Kendrick B; Kreilgârd L; Matsuura J; Manning MC; Carpenter JF
Arch Biochem Biophys; 1997 Nov; 347(2):213-20. PubMed ID: 9367527
[TBL] [Abstract][Full Text] [Related]
4. Differences in conformational dynamics of ribonucleases A and S as observed by infrared spectroscopy and hydrogen-deuterium exchange.
Dong A; Hyslop RM; Pringle DL
Arch Biochem Biophys; 1996 Sep; 333(1):275-81. PubMed ID: 8806781
[TBL] [Abstract][Full Text] [Related]
5. Two-dimensional near-IR correlation spectroscopy study of molten globule-like state of ovalbumin in acidic pH region: simultaneous changes in hydration and secondary structure.
Murayama K; Ozaki Y
Biopolymers; 2002; 67(6):394-405. PubMed ID: 12209447
[TBL] [Abstract][Full Text] [Related]
6. Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy.
Reinstädler D; Fabian H; Backmann J; Naumann D
Biochemistry; 1996 Dec; 35(49):15822-30. PubMed ID: 8961946
[TBL] [Abstract][Full Text] [Related]
7. Protein structural segments and their interconnections derived from optical spectra. Thermal unfolding of ribonuclease T1 as an example.
Pancoska P; Fabian H; Yoder G; Baumruk V; Keiderling TA
Biochemistry; 1996 Oct; 35(40):13094-106. PubMed ID: 8855946
[TBL] [Abstract][Full Text] [Related]
8. Amide I two-dimensional infrared spectroscopy of proteins.
Ganim Z; Chung HS; Smith AW; Deflores LP; Jones KC; Tokmakoff A
Acc Chem Res; 2008 Mar; 41(3):432-41. PubMed ID: 18288813
[TBL] [Abstract][Full Text] [Related]
9. Cross-strand coupling and site-specific unfolding thermodynamics of a trpzip beta-hairpin peptide using 13C isotopic labeling and IR spectroscopy.
Huang R; Wu L; McElheny D; Bour P; Roy A; Keiderling TA
J Phys Chem B; 2009 Apr; 113(16):5661-74. PubMed ID: 19326892
[TBL] [Abstract][Full Text] [Related]
10. A quantitative reconstruction of the amide I contour in the IR spectra of globular proteins: from structure to spectrum.
Brauner JW; Flach CR; Mendelsohn R
J Am Chem Soc; 2005 Jan; 127(1):100-9. PubMed ID: 15631459
[TBL] [Abstract][Full Text] [Related]
11. Temperature-induced unfolding of ribonuclease A embedded in spherical polyelectrolyte brushes.
Wittemann A; Ballauff M
Macromol Biosci; 2005 Jan; 5(1):13-20. PubMed ID: 15633159
[TBL] [Abstract][Full Text] [Related]
12. Hydrogen exchange in ribonuclease A and ribonuclease S: evidence for residual structure in the unfolded state under native conditions.
Neira JL; Sevilla P; Menéndez M; Bruix M; Rico M
J Mol Biol; 1999 Jan; 285(2):627-43. PubMed ID: 9878434
[TBL] [Abstract][Full Text] [Related]
13. Secondary structure of the exchange-resistant core from the nicotinic acetylcholine receptor probed directly by infrared spectroscopy and hydrogen/deuterium exchange.
Méthot N; Baenziger JE
Biochemistry; 1998 Oct; 37(42):14815-22. PubMed ID: 9778355
[TBL] [Abstract][Full Text] [Related]
14. Thermally induced hydrogen exchange processes in small proteins as seen by FTIR spectroscopy.
Backmann J; Schultz C; Fabian H; Hahn U; Saenger W; Naumann D
Proteins; 1996 Mar; 24(3):379-87. PubMed ID: 8778785
[TBL] [Abstract][Full Text] [Related]
15. Residual structure in unfolded proteins revealed by Raman optical activity.
Wilson G; Hecht L; Barron LD
Biochemistry; 1996 Sep; 35(38):12518-25. PubMed ID: 8823188
[TBL] [Abstract][Full Text] [Related]
16. Thermal denaturation of Escherichia coli thioredoxin studied by hydrogen/deuterium exchange and electrospray ionization mass spectrometry: monitoring a two-state protein unfolding transition.
Maier CS; Schimerlik MI; Deinzer ML
Biochemistry; 1999 Jan; 38(3):1136-43. PubMed ID: 9894011
[TBL] [Abstract][Full Text] [Related]
17. Infrared and circular dichroism spectroscopic characterization of structural differences between beta-lactoglobulin A and B.
Dong A; Matsuura J; Allison SD; Chrisman E; Manning MC; Carpenter JF
Biochemistry; 1996 Feb; 35(5):1450-7. PubMed ID: 8634275
[TBL] [Abstract][Full Text] [Related]
18. Structural study of the catalytic domain of PKCzeta using infrared spectroscopy and two-dimensional infrared correlation spectroscopy.
Sánchez-Bautista S; Kazaks A; Beaulande M; Torrecillas A; Corbalán-García S; Gómez-Fernández JC
FEBS J; 2006 Jul; 273(14):3273-86. PubMed ID: 16792700
[TBL] [Abstract][Full Text] [Related]
19. Water penetration into protein secondary structure revealed by hydrogen-deuterium exchange two-dimensional infrared spectroscopy.
DeFlores LP; Tokmakoff A
J Am Chem Soc; 2006 Dec; 128(51):16520-1. PubMed ID: 17177399
[TBL] [Abstract][Full Text] [Related]
20. Two-dimensional infrared spectroscopy of antiparallel beta-sheet secondary structure.
Demirdöven N; Cheatum CM; Chung HS; Khalil M; Knoester J; Tokmakoff A
J Am Chem Soc; 2004 Jun; 126(25):7981-90. PubMed ID: 15212548
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]