Institution
Laboratory of Molecular Biology
Facility•Cambridge, Cambridgeshire, United Kingdom•
About: Laboratory of Molecular Biology is a facility organization based out in Cambridge, Cambridgeshire, United Kingdom. It is known for research contribution in the topics: Gene & RNA. The organization has 19395 authors who have published 24236 publications receiving 2101480 citations.
Topics: Gene, RNA, DNA, Population, Receptor
Papers published on a yearly basis
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TL;DR: The hydrophobic bond is the term used by Kauzmann to describe the gain in free energy on the transfer of non-polar residues from an aqueous environment to the interior of proteins.
Abstract: THE hydrophobic bond is the term used by Kauzmann1 to describe the gain in free energy on the transfer of non-polar residues from an aqueous environment to the interior of proteins. This has been accepted as one of the major forces involved in the folding of proteins. The exact origin of the energy of the hydrophobic bond is controversial2, but empirical values have been derived for 10 protein residue side chains by Nozaki and Tanford3 who measured the solubility of amino acids in the organic solvents ethanol and dioxane.
830 citations
TL;DR: It is proposed that the function of dream sleep is to remove certain undesirable modes of interaction in networks of cells in the cerebral cortex by a reverse learning mechanism, so that the trace in the brain of the unconscious dream is weakened, rather than strengthened, by the dream.
Abstract: We propose that the function of dream sleep (more properly rapid-eye movement or REM sleep) is to remove certain undesirable modes of interaction in networks of cells in the cerebral cortex. We postulate that this is done in REM sleep by a reverse learning mechanism (see also p. 158), so that the trace in the brain of the unconscious dream is weakened, rather than strengthened, by the dream.
826 citations
TL;DR: Assessment of antibody-antigen association kinetics showed that D1.3 and most of the reshaped antibodies had bimolecular rate constants of 1.4 x 10(6) s-1 M-1, indicating that differences in equilibrium constant were predominantly due to different rates of dissociation of lysozyme from immune complexes.
825 citations
822 citations
TL;DR: An analysis of 15 protein structures indicates: first, the loss of accessible surface area by monomeric proteins on folding—proportional to hydrophobic energy—is a simple function of molecular weight.
Abstract: An analysis of 15 protein structures indicates: First, the loss of accessible surface area by monomeric proteins on folding-proportional to hydrophobic energy-is a simple function of molecular weight; second, the proportion of polar groups forming intramolecular hydrogen bonds is constant; and third, protein interiors are closely packed, each residue occupying the same volume as it does in crystals of amino acids.
815 citations
Authors
Showing all 19431 results
| Name | H-index | Papers | Citations |
|---|---|---|---|
| Robert J. Lefkowitz | 214 | 860 | 147995 |
| Ronald M. Evans | 199 | 708 | 166722 |
| Tony Hunter | 175 | 593 | 124726 |
| Marc G. Caron | 173 | 674 | 99802 |
| Mark Gerstein | 168 | 751 | 149578 |
| Timothy A. Springer | 167 | 669 | 122421 |
| Harvey F. Lodish | 165 | 782 | 101124 |
| Ira Pastan | 160 | 1286 | 110069 |
| Bruce N. Ames | 158 | 506 | 129010 |
| Philip Cohen | 154 | 555 | 110856 |
| Gerald M. Rubin | 152 | 382 | 115248 |
| Ashok Kumar | 151 | 5654 | 164086 |
| Kim Nasmyth | 142 | 294 | 59231 |
| Kenneth M. Yamada | 139 | 446 | 72136 |
| Harold E. Varmus | 137 | 496 | 76320 |