Influence of thermal motion on 1H chemical shifts in proteins: the case of bovine pancreatic trypsin inhibitor.
The possible influence of thermal motion on 1H chemical shifts is discussed for a small stable protein, the bovine pancreatic Kunitz trypsin inhibitor (BPTI). The thermal effects on the aromatic side chains and on the backbone are treated separately. The thermal motion of the aromatic side chains is accounted for in terms of their rotation around the C(alpha)-C(beta) bond and the motion of each individual proton is interpreted as a ratio between the amount of ordered and quite disordered states. The influence of hydrogen bonds is introduced as an extra contribution to the chemical shifts of the bonded proton. Their contribution to the chemical shifts resulting from the polarization of the peptide bond is investigated, as is their influence on local flexibility. Finally, the relative importance of each contribution to the chemical shift information is compared.
Busetta
B
B
Unité de Biophysique Structurale (UMR 5471-CNRS), Université Bordeaux I, Talence, France.
Picard
P
P
Precigoux
G
G
D000818:Animals; D002417:Cattle; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008956:Models, Chemical; D010179:Pancreas / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D011522:Protons; D013696:Temperature; D014361:Trypsin Inhibitors; D000516:alpha-Amylases / Q000037:antagonists & inhibitors
D010940:Plant Proteins; D011506:Proteins; D011522:Protons; D014361:Trypsin Inhibitors; D000516:alpha-Amylases