Mixed trehalose/sucrose glasses used for protein incorporation as studied by infrared and optical spectroscopy

Analytical Biochemistry

Volumn 307, Issue 1, 2002, Pages 167-172

  Wright, Wayne W ^a   Carlos Baez, Juan ^a   Vanderkooi, Jane M ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDES; AMINO ACIDS; BENDING (FORMING); GLASS; INFRARED SPECTROSCOPY; PROTEINS;

LIVER ALCOHOL DEHYDROGENASE; OPTICAL SPECTROSCOPY; OPTICALLY CLEAR; OXYGEN DIFFUSION; SECONDARY STRUCTURES; TEMPERATURE CHANGES; TEMPERATURE RANGE; WIDE TEMPERATURE RANGES;

GLASS BONDING;

ALCOHOL DEHYDROGENASE; LIVER ENZYME; PARVALBUMIN; SUCROSE; TREHALOSE; TRYPTOPHAN DERIVATIVE; DRUG DERIVATIVE; GLASS; N ACETYLTRYPTOPHAN; N-ACETYLTRYPTOPHANAMIDE; OXYGEN; TRYPTOPHAN; WATER;

ARTICLE; HYDROGEN BOND; INFRARED SPECTROSCOPY; OXYGEN DIFFUSION; PHOSPHORESCENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN IMMOBILIZATION; PROTEIN SECONDARY STRUCTURE; ROOM TEMPERATURE; TEMPERATURE DEPENDENCE; ULTRAVIOLET SPECTROSCOPY; ANIMAL; CHEMISTRY; CRYSTALLIZATION; ENZYMOLOGY; FISH; FREEZE DRYING; HORSE; INFRARED SPECTROPHOTOMETRY; LIVER; METABOLISM; PHOSPHORYLATION; SPECTROPHOTOMETRY; THERMODYNAMICS;

ALCOHOL DEHYDROGENASE; ANIMALS; CRYSTALLIZATION; FISHES; FREEZE DRYING; GLASS; HORSES; HYDROGEN BONDING; LIVER; OXYGEN; PARVALBUMINS; PHOSPHORYLATION; PROTEIN STRUCTURE, SECONDARY; SPECTROPHOTOMETRY; SPECTROPHOTOMETRY, INFRARED; SUCROSE; THERMODYNAMICS; TREHALOSE; TRYPTOPHAN; WATER;

EID: 0036678070     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(02)00034-9     Document Type: Article

References (33)

1. Is trehalose special for preserving dry biomaterials?
2. Solvent viscosity and the dynamics of dioxygen binding to myoglobin
3. A reduction of protein specific motions in CO-ligated myoglobin embedded in a trehalose glass
4. Protein reaction kinetics in a room-temperature glass
5. Room temperature phosphorescence from tryptophan and halogenated tryptophan analogs in amorphous sucrose
6. Experimental simulation of macromolecules in trehalose aqueous solutions: A photon correlation spectroscopy study
7. Phase relations and vitrification in saccharide-water solutions and the trehalose anomaly
8. α, α-Trehalose-water solutions. 3. Vibrational dynamics studies by inelastic light scattering
9. Fragile-like behavior and H-bond interactions of the glass-forming water-trehalose system
10. On the prevalence of room temperature protein phosphorescence
11. Excited triplet states used to study biological macromolecules at room temperature
12. Tryptophan phosphorescence at room temperature as a tool to study protein structure and dynamics
13. Dynamics of parvalbumin studied by fluorescence emission and triplet absorption spectroscopy of tryptophan
14. Infrared spectroscopic study on the properties of the anhydrous form II of trehalose: Implications for the functional mechanism of trehalose as a biostabilizer
15. 2+-binding proteins: Marker bands for identifying the types of coordination of the side-chain COO- groups to metal ions in pike parvalbumin (p1 = 4.10)
16. Conformational effects of calcium release from parvalbumin: Comparison of computational simulations with spectroscopic investigations
17. An infrared spectroscopic study of the interactions of carbohydrates with dried proteins
18. Optical spectra of FeII cytochrome c interpreted using molecular dynamics simulations and quantum mechanical calculations
19. Luminescence of polypeptides and Proteins
20. Infrared spectra of amide groups in α-helical proteins: Evidence for hydrogen bonding to water
21. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
22. The energy landscapes and motions of proteins
23. Dynamical transition of myoglobin revealed by ineleastic neutron scattering
24. Native protein fluctuations: The conformational-motion temperature and the inverse correlation of protein flexibility with protein stability
25. The inverse relationship between protein dynamics and thermal stability
26. Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature
27. The indole nucleus triplet-state lifetime and its dependence on solvent microviscosity
28. Characterization of tryptophan environments in glutamate dehydrogenases from temperature-dependent phosphorescence
29. Quenching of room temperature protein phosphorescence by added small molecules
30. Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence
31. Quenching of Tryptophan Phosphorescence in Escherichia coli alkaline phosphatase by long-range transfer mechanisms to external agents in the rapid-diffusion limit
32. Hydrogen exchange at the core of Escherichia coli alkaline phosphatase studied by room-temperature tryptophan phosphorescence