Trans-membrane proteins represent highly interesting and important objects still far from deep recognition. They are playing different and specific biological roles which appear to be highly structure-dependent. The mechanism of their anchorage in the membrane remains unclear mostly due to altered versus water proteins affinity of their polypeptides to the environment. They do, however, occupy a key position in the cells of organisms. This is why every attempt to elucidate details of folding, localization and their function are greatly anticipated. Additionally, the wide spectrum of biological function makes this group of proteins of special interest. Simple support to channels function and highly complicated receptor functions, which control the information signals transport between external surroundings with all processes running in the interior of cell make membrane and trans-membrane proteins particularly critical for the majority of cell processes.
Membrane proteins and trans-membrane proteins rise in particular the problem of the influence of the external force field on the protein folding process. Polar surrounding of water impels hydrophobic residues to central area of protein forming in this way hydrophobic core. In contrast membrane environment directs hydrophobic residues to protein surface, If the membrane proteins are designed to play the role of trans-membrane channels central part of such protein becomes empty. It makes such structures complicated additionally. This is why every new information taking into account high structural diversity of such proteins is highly expected. The issue is however open for all aspects of the problem and all coming new information will be highly appreciated.
We welcome Original Research, Review, Mini Review and Perspective articles on themes including, but not limited to:
• Secondary structure preferences
• Tertiary structure preferences
• Role of external field in structure generation
• Significance of mutations and their influence on biological activity
• Degradation of membrane proteins
• Is it possible to recognise the target environment on the basis of amino acid sequence ?
• Practical applicability to medicine – for instance antibiotic therapy
• Differentiation related to the transported molecule/signal
• Connexins – specificity allowing cell-to-cell junction
• Analysis of structure and function of proteins and as well These involved in relation of proteins and environment
• Studies expressing the influence of the environment on protein folding taking into account both the water and hydrophobic surrounding in the form of external force field
Trans-membrane proteins represent highly interesting and important objects still far from deep recognition. They are playing different and specific biological roles which appear to be highly structure-dependent. The mechanism of their anchorage in the membrane remains unclear mostly due to altered versus water proteins affinity of their polypeptides to the environment. They do, however, occupy a key position in the cells of organisms. This is why every attempt to elucidate details of folding, localization and their function are greatly anticipated. Additionally, the wide spectrum of biological function makes this group of proteins of special interest. Simple support to channels function and highly complicated receptor functions, which control the information signals transport between external surroundings with all processes running in the interior of cell make membrane and trans-membrane proteins particularly critical for the majority of cell processes.
Membrane proteins and trans-membrane proteins rise in particular the problem of the influence of the external force field on the protein folding process. Polar surrounding of water impels hydrophobic residues to central area of protein forming in this way hydrophobic core. In contrast membrane environment directs hydrophobic residues to protein surface, If the membrane proteins are designed to play the role of trans-membrane channels central part of such protein becomes empty. It makes such structures complicated additionally. This is why every new information taking into account high structural diversity of such proteins is highly expected. The issue is however open for all aspects of the problem and all coming new information will be highly appreciated.
We welcome Original Research, Review, Mini Review and Perspective articles on themes including, but not limited to:
• Secondary structure preferences
• Tertiary structure preferences
• Role of external field in structure generation
• Significance of mutations and their influence on biological activity
• Degradation of membrane proteins
• Is it possible to recognise the target environment on the basis of amino acid sequence ?
• Practical applicability to medicine – for instance antibiotic therapy
• Differentiation related to the transported molecule/signal
• Connexins – specificity allowing cell-to-cell junction
• Analysis of structure and function of proteins and as well These involved in relation of proteins and environment
• Studies expressing the influence of the environment on protein folding taking into account both the water and hydrophobic surrounding in the form of external force field
