Folding of polypeptide chains in proteins: a proposed mechanism for folding.

نویسندگان

  • P N Lewis
  • F A Momany
  • H A Scheraga
چکیده

A mechanism is proposed for the folding of protein chains. On the basis of short-range interactions, certain aminoacid sequences have a high propensity to be, say, alpha-helical. However, these short helical (or other ordered) regions can be stabilized only by long-range interactions arising from the proximity of two such ordered regions. These regions are brought near each other by the directing influence of certain other aminoacid sequences that have a high probability of forming beta-bends or variants thereof, also on the basis of short-range interactions. An analysis is made of the tendency of various amino acids to occur in beta-bends, and it is possible to predict the regions of a chain in which a beta-bend will occur with a high degree of reliability.

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Determine folding mechanism of Lali structure, northern Dezful, Zagros, Iran

     Lali sub-surface structure, with a NW-SE Zagros trending is located in Dezful Embayment. To determine the folding mechanism, structural geometric parameters including limbs dip, amplitude, wavelength, and crestal length were determined in four stages during deformation. In order to investigate the lateral folding mechanism, these geometric parameters were analyzed in three parts in the Lal...

متن کامل

Cotranslational folding increases GFP folding yield.

Protein sequences evolved to fold in cells, including cotranslational folding of nascent polypeptide chains during their synthesis by the ribosome. The vectorial (N- to C-terminal) nature of cotranslational folding constrains the conformations of the nascent polypeptide chain in a manner not experienced by full-length chains diluted out of denaturant. We are still discovering to what extent the...

متن کامل

Thermostability of temperature-sensitive folding mutants of the P22 tailspike protein.

Temperature-sensitive folding mutations (tsf) of the thermostable P22 tailspike protein prevent the mutant polypeptide chain from reaching the native state at the higher end of the temperature range of bacterial growth (37-42 degrees C). At lower temperatures the mutant polypeptide chains fold and associate into native proteins. The melting temperatures of the purified native forms of seven dif...

متن کامل

Protein Stability, Folding, Disaggregation and Etiology of Conformational Malfunctions

Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. A...

متن کامل

Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding.

The trigger factor of Escherichia coli is a prolyl isomerase and accelerates proline-limited steps in protein folding with a very high efficiency. It associates with nascent polypeptide chains at the ribosome and is thought to catalyse the folding of newly synthesized proteins. In its enzymatic mechanism the trigger factor follows the Michaelis-Menten equation. The unusually high folding activi...

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

عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 68 9  شماره 

صفحات  -

تاریخ انتشار 1971