1L1000 Selection of thermolysin resistant sequence from artificial polypeptide library

نویسندگان
چکیده

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Aesthetic Fitness and Artificial Evolution for the Selection of Imagery from the Mythical Infinite Library

Aesthetic selection and artificial evolution have been two of the more successful companions introduced to the toolbox of electronic image-makers in recent years. This paper examines the niche in which this technique, often associated with the simulation of biological processes, has positioned itself and some of the reasons for its success. Some remarks concerning the meaningfulness of a user’s...

متن کامل

Selection of Specific Protein Binders for Pre-Defined Targets from an Optimized Library of Artificial Helicoidal Repeat Proteins (alphaRep)

We previously designed a new family of artificial proteins named αRep based on a subgroup of thermostable helicoidal HEAT-like repeats. We have now assembled a large optimized αRep library. In this library, the side chains at each variable position are not fully randomized but instead encoded by a distribution of codons based on the natural frequency of side chains of the natural repeats family...

متن کامل

An artificial cell-cycle inhibitor isolated from a combinatorial library.

Understanding the genetic networks that operate inside cells will require the dissection of interactions among network members. Here we describe a peptide aptamer isolated from a combinatorial library that distinguishes among such interactions. This aptamer binds to cyclin-dependent kinase 2 (Cdk2) and inhibits its kinase activity. In contrast to naturally occurring inhibitors, such as p21(Cip1...

متن کامل

Artificial polypeptide scaffold for protein immobilization.

An artificial polypeptide scaffold composed of surface anchor and protein capture domains was designed and expressed in vivo. By using a mutant E. coli phenylalanyl-tRNA synthetase, the photoreactive amino acid para-azidophenylalanine was incorporated into the surface anchor domain. Octyltrichlorosilane-treated surfaces were functionalized with this polypeptide by spin coating and photocrosslin...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Seibutsu Butsuri

سال: 2002

ISSN: 0582-4052,1347-4219

DOI: 10.2142/biophys.42.s67_3