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Journal of Molecular Biology
|
June 12, 2001
Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling
M Aslam, S J Perkins
Journal of Molecular Biology
|
March 25, 1980
Conformational transition from trypsinogen to trypsin. 1H nuclear magnetic resonance at 360 MHz and ring current calculations
S J Perkins, K Wüthrich
Journal of Molecular Biology
|
August 25, 1983
Low-resolution structural studies of mitochondrial ubiquinol:cytochrome c reductase in detergent solutions by neutron scattering
S J Perkins, H Weiss
Biochimica Et Biophysica Acta
|
February 26, 1979
Ring current effects in the conformation dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor
S J Perkins, K Wüthrich
Biochimica Et Biophysica Acta
|
October 23, 1978
Structural interpretation of lanthanide binding to the basic pancreatic trypsin inhibitor by 1H NMR at 360 MHz
S J Perkins, K Wüthrich
Journal of Molecular Biology
|
September 1, 2000
Conformational changes during the assembly of factor B from its domains by (1)H NMR spectroscopy and molecular modelling: their relevance to the regulation of factor B activity
J Hinshelwood, S J Perkins
European Journal of Biochemistry
|
May 15, 1986
Molecular modelling of human complement component C3 and its fragments by solution scattering
S J Perkins, R B Sim
Journal of Molecular Biology
|
July 12, 1996
Assessment of protein fold predictions from sequence information: the predicted alpha/beta doubly wound fold of the von Willebrand factor type A domain is similar to its crystal structure
Y J Edwards, S J Perkins
FEBS Letters
|
June 17, 1996
The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily
N C Brissett, S J Perkins
Biochemistry
|
January 22, 1980
Comparisons of ring-current shifts calculated from the crystal structure of egg white lysozyme of hen with the proton nuclear magnetic resonance spectrum of lysozyme in solution
S J Perkins, R A Dwek
Page
of 13
Search research articles
Search
Showing results (11-20 of 123) with videos related to
Sort By:
Page
of 13
Journal of Molecular Biology
|
June 12, 2001
Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling
M Aslam, S J Perkins
Journal of Molecular Biology
|
March 25, 1980
Conformational transition from trypsinogen to trypsin. 1H nuclear magnetic resonance at 360 MHz and ring current calculations
S J Perkins, K Wüthrich
Journal of Molecular Biology
|
August 25, 1983
Low-resolution structural studies of mitochondrial ubiquinol:cytochrome c reductase in detergent solutions by neutron scattering
S J Perkins, H Weiss
Biochimica Et Biophysica Acta
|
February 26, 1979
Ring current effects in the conformation dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor
S J Perkins, K Wüthrich
Biochimica Et Biophysica Acta
|
October 23, 1978
Structural interpretation of lanthanide binding to the basic pancreatic trypsin inhibitor by 1H NMR at 360 MHz
S J Perkins, K Wüthrich
Journal of Molecular Biology
|
September 1, 2000
Conformational changes during the assembly of factor B from its domains by (1)H NMR spectroscopy and molecular modelling: their relevance to the regulation of factor B activity
J Hinshelwood, S J Perkins
European Journal of Biochemistry
|
May 15, 1986
Molecular modelling of human complement component C3 and its fragments by solution scattering
S J Perkins, R B Sim
Journal of Molecular Biology
|
July 12, 1996
Assessment of protein fold predictions from sequence information: the predicted alpha/beta doubly wound fold of the von Willebrand factor type A domain is similar to its crystal structure
Y J Edwards, S J Perkins
FEBS Letters
|
June 17, 1996
The protein fold of the hyaluronate-binding proteoglycan tandem repeat domain of link protein, aggrecan and CD44 is similar to that of the C-type lectin superfamily
N C Brissett, S J Perkins
Biochemistry
|
January 22, 1980
Comparisons of ring-current shifts calculated from the crystal structure of egg white lysozyme of hen with the proton nuclear magnetic resonance spectrum of lysozyme in solution
S J Perkins, R A Dwek
Page
of 13