Publisher Summary This chapter reviews that the simplest way of accounting for the absorption spectrum of a protein is as the sum of the spectra of its components. This gives results which are often good approximations to the observed protein spectrum. The assumption of additivity is basic for useful analytical applications of spectral measurements. It discusses that in another perspective, the failure of perfect additivity of the component absorptivities affords the possibility of obtaining structural information about proteins. The absorptivity of the peptide bond can change by as much as a factor of two with a change in the conformation of a peptide chain. Since the absorptivity of aromatic side chains is much less sensitive to environmental change, correspondingly, more sensitive techniques are required to measure the small changes which do occur. The nature and limitations of the structural information resulting from both peptide-bond and side-chain absorption are discussed. Absorption spectra can occasionally be a useful tool in the identification of unusual structural features in proteins and polypeptides. Several such applications are also explained in this chapter.

Ultraviolet spectra Of Proteins and Amino Acids

Publisher Summary This chapter reviews the physical, chemical, and biological properties of insulin in the light of the atomic arrangement found in insulin crystals. It also describes the relation of the three-dimensional arrangement of the atoms in the molecule of 2-zinc insulin crystal to the solution properties of insulin (particularly its states of aggregation), to the chemical reaction and chemical modification of the molecule, and to its primary biological activity. Normally the insulin crystals contain two zinc ions to every six molecules of insulin—a hexamer. The slow solution of the crystals provides a method of delaying the action of insulin that closely parallels the methods adopted in the pancreas itself for the storage and release of insulin. Within many β granules, grains can be seen that almost certainly contain zinc insulin hexamers packed in a crystalline array, and in experimental animals diabetes has been induced by chelating agents, such as EDTA, perhaps simply by interfering with normal insulin storage. It, therefore, seems plausible that ready crystallization of insulin in the presence of zinc is a reflection of the storage processes in the β cell.

Insulin: The Structure in the Crystal and its Reflection in Chemistry and Biology by

Interpretation of the ultraviolet spectral changes of proteins.

States of amino acid residues in proteins

Isolation and characterization of products formed by the action of trypsin on insulin.

ウシ結晶亜鉛インシュリンと脱亜鉛インシュリン中のチロシンの水素結合の状態。トリプシン,カルボキシペプチダーゼ消化,ならびに酸性化の際にみられる吸収スペクトルの変化の測定による

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ウシ結晶亜鉛インシュリンと脱亜鉛インシュリン中のチロシンの水素結合の状態。トリプシン,カルボキシペプチダーゼ消化,ならびに酸性化の際にみられる吸収スペクトルの変化の測定による