In many important types of observations in biological research, the information provided by the specimens is in the form of photons-quanta of visible light, u.v., or X-rays. The process of observation becomes one of recording this information in useful form, with as high an efficiency as possible. The problem becomes particularly important when for some reason or other the total number or rate of quanta provided by the specimen is small. Examples of such limitations are included in the following: (i) Processes permitting only low-intensity illumination in order not to interfere with the biological processes under observation. (ii) Processes changing very rapidly and requiring rapid sequence recording. (iii) Processes providing only a limited number of photons per event, such as bioluminescence. (iv) Processes in which radioactive tracers are utilized, and observation of radioactivity is desirable at low specific activity or within short time intervals. (v) X-ray diffraction processes where the specimen is weakly diffracting or where the X-ray intensity must be kept low in order not to damage the specimen. (vi) Processes involving the observation of fluorescence, where the intensity is low because of limitations on the amount of tagging material.

Visual pigments are embedded in the disc membranes of the outer segments of vertebrate rods and cones and in the microvilli of invertebrate visual cells. The pigment molecule in both is a most fascinating aggregate of known (the ubiquitous II-cis isomer of vitamin A1 or A2-aldehyde = retinal1 or 2; Hubbard & Wald, 1952) covalently bonded to the unknown (a protein termed opsin) (Anderson, Hoffman & Hall, 1971). This conjugated molecule is called rhodopsin or dehydrorhodopsin (porphryopsin) when the prosthetic portion is retinall or 2 respectively. So sensitive is this sterically hindered, bent and twisted molecule to light that absorption of one photon can initiate its isomerization to the all trans form. This conformational change is but one (but the best known) of the factors leading to receptor membrane changes ushering in the visual impulse.

Several cases of modifications of functional properties of proteins upon specific interaction with antibodies have been reported in the last few years. The purpose of this paper is to discuss evidence that these effects may be due to conformational changes in the protein molecule.