4RAT

EFFECTS OF TEMPERATURE ON PROTEIN STRUCTURE AND DYNAMICS: X-RAY CRYSTALLOGRAPHIC STUDIES OF THE PROTEIN RIBONUCLEASE-A AT NINE DIFFERENT TEMPERATURES FROM 98 TO 320 K

Summary for 4RAT

• Entry DOI: 10.2210/pdb4rat/pdb
• Descriptor: RIBONUCLEASE A (1 entity in total)
• Functional Keywords: hydrolase (nucleic acid, rna)
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P61823
• Total number of polymer chains: 1
• Total formula weight: 13708.33

Authors

Tiltonjunior, R.F.,Dewan, J.C.,Petsko, G.A. (deposition date: 1991-08-13, release date: 1993-07-15, Last modification date: 2024-10-30)

Primary citation

Tilton Jr., R.F.,Dewan, J.C.,Petsko, G.A.
Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K.
Biochemistry, 31:2469-2481, 1992

PubMed Abstract: Structures using X-ray diffraction data collected to 1.5-A resolution have been determined for the protein ribonuclease-A at nine different temperatures ranging from 98 to 320 K. It is determined that the protein molecule expands slightly (0.4% per 100 K) with increasing temperature and that this expansion is linear. The expansion is due primarily to subtle repacking of the molecule, with exposed and mobile loop regions exhibiting the largest movements. Individual atomic Debye-Waller factors exhibit predominantly biphasic behavior, with a small positive slope at low temperatures and a larger positive slope at higher temperatures. The break in this curve occurs at a characteristic temperature of 180-200 K, perhaps indicative of fundamental changes in the dynamical structure of the surrounding protein solvent. The distribution of protein Debye-Waller factors is observed to broaden as well as shift to higher values as the temperature is increased.

PubMed: 1547232
DOI: 10.1021/bi00124a006

Experimental method

X-RAY DIFFRACTION (1.5 Å)