SOME STUDIES ON THE INFRARED ABSORPTION OF THE CONTRACTILE SYSTEM OF SKELETAL MUSCLE

[1] NEW EVIDENCE ON THE STRUCTURE OF SOME PROTEINS FROM MEASUREMENTS WITH POLARIZED INFRA-RED RADIATION [J]. NATURE, 1949, 163 (4153) : 859 - 862

[2] STUDIES OF THE STRUCTURE OF SYNTHETIC POLYPEPTIDES [J]. NATURE, 1948, 162 (4120) : 596 - 600

[3] INFRA-RED SPECTROSCOPY WITH THE REFLECTING MICROSCOPE IN PHYSICS, CHEMISTRY AND BIOLOGY [J]. NATURE, 1949, 163 (4136) : 198 - 201

[4] BARNES RB, 1949, ANAL CHEM, V21, P7, DOI DOI 10.1021/AC60025A003

[5] INFRARED SPECTRA OF TISSUES [J]. SCIENCE, 1949, 110 (2849) : 137 - 138

[6] BLOUT ER, 1949, J BIOL CHEM, V178, P335

[7] THE ELASTIC MECHANISM AND HYDROGEN BONDING IN ACTOMYOSIN THREADS [J]. JOURNAL OF CELLULAR AND COMPARATIVE PHYSIOLOGY, 1951, 37 (01): : 27 - 55

[8] BUCHTHAL F, 1949, ACTA PHYSIOL SCAND, V16, P326

[9] DAASCH L, UNPUB

[10] Studies on the anomalous viscosity and flow-birefringence of protein solutions III. Changes in these properties of myosin solutions in relation to adenosinetriphosphate and muscular contraction [J]. JOURNAL OF GENERAL PHYSIOLOGY, 1944, 27 (04) : 355 - 399

[1] NEW EVIDENCE ON THE STRUCTURE OF SOME PROTEINS FROM MEASUREMENTS WITH POLARIZED INFRA-RED RADIATION [J]. NATURE, 1949, 163 (4153) : 859 - 862

[2] STUDIES OF THE STRUCTURE OF SYNTHETIC POLYPEPTIDES [J]. NATURE, 1948, 162 (4120) : 596 - 600

[3] INFRA-RED SPECTROSCOPY WITH THE REFLECTING MICROSCOPE IN PHYSICS, CHEMISTRY AND BIOLOGY [J]. NATURE, 1949, 163 (4136) : 198 - 201

[4] BARNES RB, 1949, ANAL CHEM, V21, P7, DOI DOI 10.1021/AC60025A003

[5] INFRARED SPECTRA OF TISSUES [J]. SCIENCE, 1949, 110 (2849) : 137 - 138

[6] BLOUT ER, 1949, J BIOL CHEM, V178, P335

[7] THE ELASTIC MECHANISM AND HYDROGEN BONDING IN ACTOMYOSIN THREADS [J]. JOURNAL OF CELLULAR AND COMPARATIVE PHYSIOLOGY, 1951, 37 (01): : 27 - 55

[8] BUCHTHAL F, 1949, ACTA PHYSIOL SCAND, V16, P326

[9] DAASCH L, UNPUB

[10] Studies on the anomalous viscosity and flow-birefringence of protein solutions III. Changes in these properties of myosin solutions in relation to adenosinetriphosphate and muscular contraction [J]. JOURNAL OF GENERAL PHYSIOLOGY, 1944, 27 (04) : 355 - 399