Effects of temperature and pH on prothrombin fragment 1 conformation as determined by nuclear magnetic resonance

Biochemistry ◽  
1981 ◽  
Vol 20 (21) ◽  
pp. 6149-6155 ◽  
Author(s):  
Carol H. Pletcher ◽  
Elene F. Bouhoutsos-Brown ◽  
Robert G. Bryant ◽  
Gary L. Nelsestuen
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Prothrombin Fragment ◽  
Effects Of Temperature ◽  
Nuclear Magnetic

scholarly journals Effects of temperature on Rb and 129Xe spin polarization in a nuclear magnetic resonance gyroscope with low pump power

AIP Advances ◽  
2017 ◽  
Vol 7 (11) ◽  
pp. 115101 ◽  
Author(s):  
Linlin Chen ◽  
Binquan Zhou ◽  
Guanqun Lei ◽  
Wenfeng Wu ◽  
Yueyang Zhai ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Pump Power ◽  
Magnetic Resonance ◽  
Spin Polarization ◽  
Effects Of Temperature ◽  
Nuclear Magnetic

Solution Studio of Bovins Prothrombin Fragments Using high Resolution Nuclear Magnetic Resonance Spectroscopy

1979 ◽  
Author(s):  
M.P. Esnouf ◽  
E.A. Israel ◽  
N.D. Pluck ◽  
R.J.P. Nilliams
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
High Resolution ◽  
Magnetic Resonance Spectroscopy ◽  
Nuclear Magnetic Resonance Spectroscopy ◽  
Tertiary Structure ◽  
Random Coil ◽  
Resonance Spectroscopy ◽  
Prothrombin Fragment ◽  
Nuclear Magnetic

High resolution nuclear magnetic resonance spectroscopy (NMR) is now a widely used technique for investigating the solution structures of proteins. In particular, proton NMR provides information on the entire molecular structure and is not confined to the study of a few amino acid side chains with specific properties. We have used this technique (at 270 MHz) to investigate the solution behaviour of bovine prothrombin fragment 1. Large variations in temperature and pH are seen to have little or no effect on its spectrum. Indeed, the spectra are all very similar to those expected for a “random coil” protein. The protein has little tertiary structure. Calcium binding has been monitored and small changes involving tryptophan intensity have been seen in agreement with the results of other physical methods. However, NMR shows there to be no significant change in tertiary structure in fragment 1 on binding calcium. Prothrombin fragment 2 contains the second Kringle region - a large amount of its sequence being homologous to that in fragment 1. Preliminary experiments have shown bovine fragment 2 to have some degree of folded structure but the temperature dependence and chemical modification studies suggest that this is not very extensive.

Interaction of lanthanide(III) ions with bovine prothrombin fragment. 1. A luminescence and nuclear magnetic resonance study

1980 ◽  
Vol 102 (10) ◽  
pp. 3413-3419 ◽  
Author(s):  
Mary E. Scott ◽  
Martha M. Sarasua ◽  
Henry C. Marsh ◽  
David L. Harris ◽  
Richard G. Hiskey ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Nuclear Magnetic Resonance Study ◽  
Magnetic Resonance Study ◽  
Prothrombin Fragment ◽  
Nuclear Magnetic

Effects of Temperature on Sorption of Water by Wheat Gluten Determined Using Deuterium Nuclear Magnetic Resonance

1999 ◽  
Vol 76 (2) ◽  
pp. 219-226 ◽  
Author(s):  
A. Grant ◽  
P. S. Belton ◽  
I. J. Colquhoun ◽  
M. L. Parker ◽  
J. J. Plijter ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Wheat Gluten ◽  
Effects Of Temperature ◽  
Nuclear Magnetic

Solution Studies Of Bovine Prothrombin Fragments Using High Resolution Nuclear Magnetic Resonance Spectroscopy

1979 ◽  
Author(s):  
M Esnouf ◽  
E Israel ◽  
N Pluck ◽  
R Williams
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
High Resolution ◽  
Magnetic Resonance Spectroscopy ◽  
Nuclear Magnetic Resonance Spectroscopy ◽  
Tertiary Structure ◽  
Random Coil ◽  
Resonance Spectroscopy ◽  
Prothrombin Fragment ◽  
Nuclear Magnetic

High resolution nuclear magnetic resonance spectroscopy (NMR) is now a widely used technique for investigating the solution structures of proteins. In particular, proton NMR provides information on the entire molecular structure and is not confined to the study of a few amino acid side chains with specific properties. We have used this technique (at 270 MHz) to investigate the solution behaviour of bovine prothrombin fragment 1. Large variations in temperature and pH are seen to have little or no effect on its spectrum. Indeed, the spectra are all very similar to those expected for a “random coil” protein. The protein has little tertiary structure. Calcium binding has been monitored and small changes involving tryptophan intensity have been seen in agreement with the results of other physical methods. However, NMR shows there to be no significant change in tertiary structure in fragment 1 on binding calcium. Prothrombin fragment 2 contains the second ,Kringle region - a large amount of its sequence being homologous to that in fragment 1. Preliminary experiments have shown bovine fragment 2 to have some degree of folded structure but the temperature dependence and chemical modification studies suggest that this is not very extensive.

An emerging technology: Nuclear magnetic resonance microscopy

1988 ◽  
Vol 46 ◽  
pp. 1000-1001
Author(s):  
M.J. Hennessy ◽  
E. Kwok
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Relaxation Times ◽  
Basic Research ◽  
Local Environment ◽  
Magnetic Resonance Images ◽  
Nmr Microscopy ◽  
Mri Scans ◽  
Temperature Relaxation ◽  
Nuclear Magnetic

Much progress in nuclear magnetic resonance microscope has been made in the last few years as a result of improved instrumentation and techniques being made available through basic research in magnetic resonance imaging (MRI) technologies for medicine. Nuclear magnetic resonance (NMR) was first observed in the hydrogen nucleus in water by Bloch, Purcell and Pound over 40 years ago. Today, in medicine, virtually all commercial MRI scans are made of water bound in tissue. This is also true for NMR microscopy, which has focussed mainly on biological applications. The reason water is the favored molecule for NMR is because water is,the most abundant molecule in biology. It is also the most NMR sensitive having the largest nuclear magnetic moment and having reasonable room temperature relaxation times (from 10 ms to 3 sec). The contrast seen in magnetic resonance images is due mostly to distribution of water relaxation times in sample which are extremely sensitive to the local environment.

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