Low-frequency internal motions in protein molecules play a key role in biological functions. A direct relationship between low-frequency motions and enzymatic activity has been suggested for bovine pancreatic ribonuclease (RNase A). The flexibility-function relationship in this enzyme has been attributed to a subtle and concerted breathing motion of the beta-sheet regions occurring upon substrate binding and release. Here, we calculate an approximate value for the force constant and the wave number of the low-frequency beta-sheet breathing motion of RNase A, by using the Boltzmann hypothesis on a set of data derived from a simple conventional structural superimposition of an unusual large number of X-ray structures available for the protein. The results agree with previous observations and with theoretical predictions on the basis of normal-mode analysis. To the best of our knowledge, this is the first example in which the wave number and the force constant of a low-frequency concerted motion in a protein are directly derived from X-ray structures.

Approximate Values for Force Constant and Wave Number Associated with a Low-Frequency Concerted Motion in Proteins Can Be Evaluated by a Comparison of X-ray Structures / Merlino, Antonello; Sica, Filomena; Mazzarella, Lelio. - In: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL. - ISSN 1520-6106. - STAMPA. - 111:(2007), pp. 5483-5486. [10.1021/jp071399h]

Approximate Values for Force Constant and Wave Number Associated with a Low-Frequency Concerted Motion in Proteins Can Be Evaluated by a Comparison of X-ray Structures.

MERLINO, ANTONELLO;SICA, FILOMENA;MAZZARELLA, LELIO
2007

Abstract

Low-frequency internal motions in protein molecules play a key role in biological functions. A direct relationship between low-frequency motions and enzymatic activity has been suggested for bovine pancreatic ribonuclease (RNase A). The flexibility-function relationship in this enzyme has been attributed to a subtle and concerted breathing motion of the beta-sheet regions occurring upon substrate binding and release. Here, we calculate an approximate value for the force constant and the wave number of the low-frequency beta-sheet breathing motion of RNase A, by using the Boltzmann hypothesis on a set of data derived from a simple conventional structural superimposition of an unusual large number of X-ray structures available for the protein. The results agree with previous observations and with theoretical predictions on the basis of normal-mode analysis. To the best of our knowledge, this is the first example in which the wave number and the force constant of a low-frequency concerted motion in a protein are directly derived from X-ray structures.
2007
Approximate Values for Force Constant and Wave Number Associated with a Low-Frequency Concerted Motion in Proteins Can Be Evaluated by a Comparison of X-ray Structures / Merlino, Antonello; Sica, Filomena; Mazzarella, Lelio. - In: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL. - ISSN 1520-6106. - STAMPA. - 111:(2007), pp. 5483-5486. [10.1021/jp071399h]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/201963
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