Low-Temperature-Induced Structural Changes in Human Lysozyme Elucidated by Three-Dimensional NMR Spectroscopy

Kumeta, Hiroyuki; Miura, Ai; Kobashigawa, Yoshihiro; Miura, Kazunori; Oka, Chitoshi; Nemoto, Nobuaki; Nitta, Katsutoshi; Tsuda, Sakae

doi:10.1021/bi026730w

Cited by 14 publications

(14 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This increase in surface area and volume with an increase in temperature seems to be a general rule for proteins (4), and likely a direct consequence of changes in temperature. The same effect was detected in the NMR structures of skeletal apo-NTnC at 30 and 4 °C (34), lysozyme at 35 and 4 °C (35), and the spruce budworm antifreeze protein at 30 and 5 °C (37), and in crystal structures of myoglobin (5), trypsin (8), ribonuclease A (9), and lysozyme (10,11).…”

Section: Discussionmentioning

confidence: 56%

Effect of Temperature on the Structure of Trout Troponin C

et al. 2004

View full text Add to dashboard Cite

Adaptation for life at different temperatures can cause changes in many aspects of an organism. One example is the expression of different protein isoforms in species adapted to different temperatures. The calcium regulatory protein cardiac troponin C (cTnC), from rainbow trout (Oncorhynchus mykiss), is a good model for studying temperature effects, both because of its low physiological temperature and because mammalian cTnC, extensively studied at higher temperatures, can be used for comparison. We determined the structure and studied the backbone dynamics of the regulatory domain of trout cardiac troponin C (ScNTnC) with one Ca(2+) bound at 7 and 30 degrees C, using nuclear magnetic resonance spectroscopy (NMR). The overall fold of the regulatory domain of trout cTnC at both temperatures is similar to the regulatory domain of mammalian (human, bovine, and porcine isoform) cTnC bound to one Ca(2+). By comparing the trout structures at the two temperatures, we identify differences between the positions of the helices flanking the calcium binding loops, and the overall structure at 7 degrees C is more compact than that at 30 degrees C. The structure at 7 degrees C is more similar to the mammalian cTnC, which was determined at 30 degrees C, indicating that they have the same conformation at their respective physiological temperatures. The dynamic properties of the regulatory domain of trout cTnC are similar at the two temperatures that were used in these studies.

show abstract

Section: Discussionmentioning

confidence: 56%

Effect of Temperature on the Structure of Trout Troponin C

et al. 2004

View full text Add to dashboard Cite

show abstract

“…Silva and Weber (45) and pressure on the size of the cavities may be obtained from the structural changes of proteins via NMR spectroscopy. This has been done for hen egg white lysozyme as a function of pressure (48) and for human lysozyme as a function of temperature (49). Some data are presented in Table 1.…”

Section: Molecular Aspects: Cavitiesmentioning

confidence: 99%

Protein dynamics: hydration and cavities

Heremans

2005

Braz J Med Biol Res

View full text Add to dashboard Cite

The temperature-pressure behavior of proteins seems to be unique among the biological macromolecules. Thermodynamic as well as kinetic data show the typical elliptical stability diagram. This may be extended by assuming that the unfolded state gives rise to volume and enthalpy-driven liquid-liquid transitions. A molecular interpretation follows from the temperature and the pressure dependence of the hydration and cavities. We suggest that positron annihilation spectroscopy can provide additional quantitative evidence for the contributions of cavities to the dynamics of proteins. Only mature amyloid fibrils that form from unfolded proteins are very resistant to pressure treatment.

show abstract

“…Recent work using NMR has addressed this question using human lysozyme as a model [21]. Recent work using NMR has addressed this question using human lysozyme as a model [21].…”

Section: Discussionmentioning

confidence: 99%

The Lysozyme from Insect (Manduca sexta) Is a Cold-Adapted Enzyme

Sotelo‐Mundo¹,

López-Zavala²,

García-Orozco³

et al. 2007

PPL

View full text Add to dashboard Cite

Enzymatic activity is dependent on temperature, although some proteins have evolved to retain activity at low temperatures at the expense of stability. Cold adapted enzymes are present in a variety of organisms and there is ample interest in their structure-function relationships. Lysozyme (E.C. 3.2.1.17) is one of the most studied enzymes due to its antibacterial activity against Gram positive bacteria and is also a cold adapted protein. In this work the characterization of lysozyme from the insect Manduca sexta and its activity at low temperatures is presented. Both M. sexta lysozymes natural and recombinant showed a higher content of alpha-helix secondary structure compared to that of hen egg white lysozyme and a higher specific enzymatic activity in the range of 5-30 degrees C. These results together with measured thermodynamic activation parameters support the designation of M. sexta lysozyme as a cold adapted enzyme. Therefore, the insect recombinant lysozyme is feasible as a model for structure-function studies for cold-adapted proteins.

show abstract

Low-Temperature-Induced Structural Changes in Human Lysozyme Elucidated by Three-Dimensional NMR Spectroscopy

Cited by 14 publications

References 39 publications

Effect of Temperature on the Structure of Trout Troponin C

Effect of Temperature on the Structure of Trout Troponin C

Protein dynamics: hydration and cavities

The Lysozyme from Insect (Manduca sexta) Is a Cold-Adapted Enzyme

Contact Info

Product

Resources

About