1rat: Difference between revisions

Revision as of 15:48, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1RAT is a Single protein structure of sequence from Bos taurus. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

ReferenceReference

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., Tilton RF Jr, Dewan JC, Petsko GA, Biochemistry. 1992 Mar 10;31(9):2469-81. PMID:1547232

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-[[Image:1rat.gif|left|200px]]<br /><applet load="1rat" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rat.gif|left|200px]]<br /><applet load="1rat" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rat, resolution 1.5&Aring;" />
 '''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'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-RAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RAT OCA].
+RAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RAT OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Pancreatic ribonuclease]]
 [[Category: Single protein]]
-[[Category: Dewan, J.C.]]
+[[Category: Dewan, J C.]]
-[[Category: Petsko, G.A.]]
+[[Category: Petsko, G A.]]
-[[Category: Tiltonjunior, R.F.]]
+[[Category: Tiltonjunior, R F.]]
 [[Category: hydrolase (nucleic acid]]
 [[Category: rna)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:25:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:48:56 2008''